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Iron in PDB 6fxq: Structure of Coproheme Decarboxylase From Listeria Monocytogenes During Turnover

Protein crystallography data

The structure of Structure of Coproheme Decarboxylase From Listeria Monocytogenes During Turnover, PDB code: 6fxq was solved by S.Hofbauer, V.Pfanzagl, G.Mlynek, D.Puehringer, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 49.00 / 1.69
Space group P 1 21 1
Cell size a, b, c (Å), α, β, γ (°) 77.687, 129.369, 77.916, 90.00, 105.52, 90.00
R / Rfree (%) 17.8 / 21.4

Other elements in 6fxq:

The structure of Structure of Coproheme Decarboxylase From Listeria Monocytogenes During Turnover also contains other interesting chemical elements:

Sodium (Na) 5 atoms

Iron Binding Sites:

The binding sites of Iron atom in the Structure of Coproheme Decarboxylase From Listeria Monocytogenes During Turnover (pdb code 6fxq). This binding sites where shown within 5.0 Angstroms radius around Iron atom.
In total 10 binding sites of Iron where determined in the Structure of Coproheme Decarboxylase From Listeria Monocytogenes During Turnover, PDB code: 6fxq:
Jump to Iron binding site number: 1; 2; 3; 4; 5; 6; 7; 8; 9; 10;

Iron binding site 1 out of 10 in 6fxq

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Iron binding site 1 out of 10 in the Structure of Coproheme Decarboxylase From Listeria Monocytogenes During Turnover


Mono view


Stereo pair view

A full contact list of Iron with other atoms in the Fe binding site number 1 of Structure of Coproheme Decarboxylase From Listeria Monocytogenes During Turnover within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Fe302

b:42.2
occ:0.38
FE A:FEC302 0.0 42.2 0.4
FE A:VOV303 0.4 40.7 0.5
N02 A:VOV303 1.9 41.5 0.5
ND A:FEC302 1.9 41.5 0.4
NC A:FEC302 2.0 45.4 0.4
N03 A:VOV303 2.0 38.6 0.5
N05 A:VOV303 2.0 45.4 0.5
NA A:FEC302 2.0 38.7 0.4
N04 A:VOV303 2.0 44.9 0.5
NB A:FEC302 2.0 45.0 0.4
NE2 A:HIS174 2.6 46.9 1.0
C4D A:FEC302 2.9 42.0 0.4
C10 A:VOV303 3.0 42.0 0.5
C1A A:FEC302 3.0 38.8 0.4
C18 A:VOV303 3.0 38.8 0.5
C07 A:VOV303 3.0 43.2 0.5
C4B A:FEC302 3.0 47.7 0.4
C43 A:VOV303 3.0 46.3 0.5
C1D A:FEC302 3.0 43.5 0.4
C1C A:FEC302 3.0 47.7 0.4
C4C A:FEC302 3.0 45.7 0.4
C21 A:VOV303 3.1 37.9 0.5
C40 A:VOV303 3.1 47.7 0.5
C32 A:VOV303 3.1 47.8 0.5
C29 A:VOV303 3.1 46.4 0.5
C4A A:FEC302 3.1 37.7 0.4
C1B A:FEC302 3.1 45.3 0.4
CHA A:FEC302 3.3 38.8 0.4
C17 A:VOV303 3.3 38.8 0.5
CHC A:FEC302 3.4 48.3 0.4
C06 A:VOV303 3.4 45.0 0.5
CHD A:FEC302 3.4 45.0 0.4
HD11 A:ILE189 3.4 53.2 1.0
C39 A:VOV303 3.4 48.4 0.5
C28 A:VOV303 3.4 40.3 0.5
CHB A:FEC302 3.5 40.4 0.4
CD2 A:HIS174 3.5 46.2 1.0
HD2 A:HIS174 3.6 55.5 1.0
HG13 A:ILE189 3.6 49.5 1.0
CE1 A:HIS174 3.7 46.4 1.0
HG3 A:GLN187 3.8 61.4 1.0
HE1 A:HIS174 3.8 55.7 1.0
CD1 A:ILE189 4.1 44.4 1.0
C09 A:VOV303 4.2 46.7 0.5
HE1 A:MET219 4.2 60.2 1.0
HHA A:FEC302 4.2 46.5 0.4
C08 A:VOV303 4.2 44.5 0.5
C3D A:FEC302 4.2 46.6 0.4
C19 A:VOV303 4.2 40.0 0.5
C2A A:FEC302 4.2 40.0 0.4
C2D A:FEC302 4.2 44.5 0.4
H171 A:VOV303 4.2 46.5 0.5
C42 A:VOV303 4.2 47.2 0.5
C20 A:VOV303 4.2 37.5 0.5
CG1 A:ILE189 4.3 41.2 1.0
C2C A:FEC302 4.3 49.2 0.4
C3B A:FEC302 4.3 49.7 0.4
C41 A:VOV303 4.3 49.6 0.5
C3C A:FEC302 4.3 47.1 0.4
HHC A:FEC302 4.3 58.0 0.4
C3A A:FEC302 4.3 37.5 0.4
C31 A:VOV303 4.3 50.2 0.5
H061 A:VOV303 4.3 54.0 0.5
C30 A:VOV303 4.3 50.7 0.5
HD12 A:ILE189 4.3 53.2 1.0
C2B A:FEC302 4.3 50.7 0.4
HHD A:FEC302 4.3 54.1 0.4
H391 A:VOV303 4.4 58.1 0.5
H281 A:VOV303 4.4 48.4 0.5
HHB A:FEC302 4.4 48.5 0.4
HG12 A:ILE189 4.4 49.5 1.0
CG A:HIS174 4.7 45.0 1.0
HE21 A:GLN187 4.7 67.4 1.0
CG A:GLN187 4.7 51.2 1.0
ND1 A:HIS174 4.8 45.3 1.0
HE2 A:MET219 4.9 60.2 1.0
CE A:MET219 4.9 50.2 1.0
HD13 A:ILE189 5.0 53.2 1.0

Iron binding site 2 out of 10 in 6fxq

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Iron binding site 2 out of 10 in the Structure of Coproheme Decarboxylase From Listeria Monocytogenes During Turnover


Mono view


Stereo pair view

A full contact list of Iron with other atoms in the Fe binding site number 2 of Structure of Coproheme Decarboxylase From Listeria Monocytogenes During Turnover within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Fe303

b:40.7
occ:0.54
FE A:VOV303 0.0 40.7 0.5
FE A:FEC302 0.4 42.2 0.4
N02 A:VOV303 2.0 41.5 0.5
N04 A:VOV303 2.0 44.9 0.5
N05 A:VOV303 2.0 45.4 0.5
ND A:FEC302 2.0 41.5 0.4
N03 A:VOV303 2.0 38.6 0.5
NC A:FEC302 2.0 45.4 0.4
NA A:FEC302 2.1 38.7 0.4
NB A:FEC302 2.1 45.0 0.4
NE2 A:HIS174 2.3 46.9 1.0
C4D A:FEC302 3.0 42.0 0.4
C10 A:VOV303 3.0 42.0 0.5
C1A A:FEC302 3.0 38.8 0.4
C4B A:FEC302 3.0 47.7 0.4
C18 A:VOV303 3.0 38.8 0.5
C32 A:VOV303 3.0 47.8 0.5
C1C A:FEC302 3.0 47.7 0.4
C40 A:VOV303 3.0 47.7 0.5
C07 A:VOV303 3.1 43.2 0.5
C43 A:VOV303 3.1 46.3 0.5
C29 A:VOV303 3.1 46.4 0.5
C21 A:VOV303 3.1 37.9 0.5
C1D A:FEC302 3.1 43.5 0.4
C4C A:FEC302 3.1 45.7 0.4
C1B A:FEC302 3.1 45.3 0.4
C4A A:FEC302 3.1 37.7 0.4
CD2 A:HIS174 3.2 46.2 1.0
HD2 A:HIS174 3.2 55.5 1.0
CHA A:FEC302 3.3 38.8 0.4
CHC A:FEC302 3.3 48.3 0.4
C17 A:VOV303 3.3 38.8 0.5
CE1 A:HIS174 3.4 46.4 1.0
C39 A:VOV303 3.4 48.4 0.5
C06 A:VOV303 3.4 45.0 0.5
C28 A:VOV303 3.5 40.3 0.5
CHD A:FEC302 3.5 45.0 0.4
CHB A:FEC302 3.5 40.4 0.4
HE1 A:HIS174 3.6 55.7 1.0
HD11 A:ILE189 3.8 53.2 1.0
HG13 A:ILE189 3.9 49.5 1.0
HE1 A:MET219 4.0 60.2 1.0
HG3 A:GLN187 4.1 61.4 1.0
HHA A:FEC302 4.2 46.5 0.4
C09 A:VOV303 4.2 46.7 0.5
HHC A:FEC302 4.2 58.0 0.4
H171 A:VOV303 4.2 46.5 0.5
C3D A:FEC302 4.2 46.6 0.4
C08 A:VOV303 4.2 44.5 0.5
C19 A:VOV303 4.2 40.0 0.5
C2A A:FEC302 4.2 40.0 0.4
C3B A:FEC302 4.2 49.7 0.4
C31 A:VOV303 4.2 50.2 0.5
C41 A:VOV303 4.3 49.6 0.5
C42 A:VOV303 4.3 47.2 0.5
C2D A:FEC302 4.3 44.5 0.4
C2C A:FEC302 4.3 49.2 0.4
C30 A:VOV303 4.3 50.7 0.5
C20 A:VOV303 4.3 37.5 0.5
H391 A:VOV303 4.3 58.1 0.5
C3C A:FEC302 4.3 47.1 0.4
C3A A:FEC302 4.3 37.5 0.4
C2B A:FEC302 4.3 50.7 0.4
H061 A:VOV303 4.4 54.0 0.5
CG A:HIS174 4.4 45.0 1.0
H281 A:VOV303 4.4 48.4 0.5
HHD A:FEC302 4.4 54.1 0.4
ND1 A:HIS174 4.4 45.3 1.0
HHB A:FEC302 4.5 48.5 0.4
CD1 A:ILE189 4.5 44.4 1.0
CG1 A:ILE189 4.6 41.2 1.0
HD12 A:ILE189 4.6 53.2 1.0
HE2 A:MET219 4.6 60.2 1.0
CE A:MET219 4.7 50.2 1.0
HG12 A:ILE189 4.7 49.5 1.0
HE21 A:GLN187 5.0 67.4 1.0

Iron binding site 3 out of 10 in 6fxq

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Iron binding site 3 out of 10 in the Structure of Coproheme Decarboxylase From Listeria Monocytogenes During Turnover


Mono view


Stereo pair view

A full contact list of Iron with other atoms in the Fe binding site number 3 of Structure of Coproheme Decarboxylase From Listeria Monocytogenes During Turnover within 5.0Å range:
probe atom residue distance (Å) B Occ
B:Fe302

b:56.7
occ:0.43
FE B:FEC302 0.0 56.7 0.4
FE B:VOV303 0.2 56.5 0.5
N05 B:VOV303 1.9 57.1 0.5
N04 B:VOV303 1.9 56.7 0.5
ND B:FEC302 1.9 58.7 0.4
NC B:FEC302 2.0 57.1 0.4
NA B:FEC302 2.0 55.9 0.4
N02 B:VOV303 2.0 59.0 0.5
NB B:FEC302 2.1 57.9 0.4
N03 B:VOV303 2.1 55.9 0.5
NE2 B:HIS174 2.9 71.1 1.0
C4D B:FEC302 2.9 59.5 0.4
C40 B:VOV303 3.0 57.3 0.5
C32 B:VOV303 3.0 58.0 0.5
C43 B:VOV303 3.0 55.9 0.5
C1A B:FEC302 3.0 55.8 0.4
C1D B:FEC302 3.0 57.9 0.4
C29 B:VOV303 3.0 57.0 0.5
C4C B:FEC302 3.0 55.9 0.4
C1C B:FEC302 3.0 57.6 0.4
C07 B:VOV303 3.1 58.5 0.5
C10 B:VOV303 3.1 59.7 0.5
C4B B:FEC302 3.1 58.1 0.4
C4A B:FEC302 3.1 55.0 0.4
C1B B:FEC302 3.1 56.9 0.4
C18 B:VOV303 3.1 56.0 0.5
C21 B:VOV303 3.1 55.1 0.5
CHA B:FEC302 3.3 58.1 0.4
C39 B:VOV303 3.3 57.4 0.5
HD2 B:HIS174 3.3 85.6 1.0
C06 B:VOV303 3.4 55.1 0.5
CHC B:FEC302 3.4 57.4 0.4
CHD B:FEC302 3.4 55.2 0.4
C17 B:VOV303 3.4 58.1 0.5
C28 B:VOV303 3.4 55.2 0.5
CD2 B:HIS174 3.5 71.3 1.0
CHB B:FEC302 3.5 55.2 0.4
HG13 B:ILE189 3.7 48.6 1.0
HD11 B:ILE189 3.8 48.6 1.0
CE1 B:HIS174 4.0 71.3 1.0
HG3 B:GLN187 4.0 62.3 1.0
C41 B:VOV303 4.2 58.0 0.5
C31 B:VOV303 4.2 60.3 0.5
C42 B:VOV303 4.2 56.4 0.5
C3D B:FEC302 4.2 61.0 0.4
C2D B:FEC302 4.2 60.9 0.4
H391 B:VOV303 4.2 68.9 0.5
HHA B:FEC302 4.2 69.7 0.4
C30 B:VOV303 4.2 59.1 0.5
C3C B:FEC302 4.2 56.4 0.4
C2C B:FEC302 4.2 58.0 0.4
C2A B:FEC302 4.2 55.6 0.4
C09 B:VOV303 4.2 61.7 0.5
C08 B:VOV303 4.2 60.9 0.5
H061 B:VOV303 4.3 66.2 0.5
C3A B:FEC302 4.3 55.1 0.4
HHC B:FEC302 4.3 68.9 0.4
HE1 B:HIS174 4.3 85.6 1.0
HHD B:FEC302 4.3 66.2 0.4
C3B B:FEC302 4.3 60.6 0.4
C19 B:VOV303 4.3 55.7 0.5
H171 B:VOV303 4.3 69.8 0.5
C20 B:VOV303 4.3 55.1 0.5
C2B B:FEC302 4.4 59.4 0.4
H281 B:VOV303 4.4 66.3 0.5
CG1 B:ILE189 4.4 40.5 1.0
HHB B:FEC302 4.4 66.3 0.4
CD1 B:ILE189 4.4 40.5 1.0
HD12 B:ILE189 4.5 48.6 1.0
HG12 B:ILE189 4.7 48.6 1.0
CG B:HIS174 4.7 67.1 1.0
HE1 B:MET219 4.8 81.4 1.0
HE2 B:MET219 4.9 81.4 1.0
HE21 B:GLN187 4.9 91.1 1.0
ND1 B:HIS174 5.0 70.2 1.0
CG B:GLN187 5.0 51.9 1.0

Iron binding site 4 out of 10 in 6fxq

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Iron binding site 4 out of 10 in the Structure of Coproheme Decarboxylase From Listeria Monocytogenes During Turnover


Mono view


Stereo pair view

A full contact list of Iron with other atoms in the Fe binding site number 4 of Structure of Coproheme Decarboxylase From Listeria Monocytogenes During Turnover within 5.0Å range:
probe atom residue distance (Å) B Occ
B:Fe303

b:56.5
occ:0.46
FE B:VOV303 0.0 56.5 0.5
FE B:FEC302 0.2 56.7 0.4
ND B:FEC302 1.9 58.7 0.4
NA B:FEC302 2.0 55.9 0.4
N02 B:VOV303 2.0 59.0 0.5
N05 B:VOV303 2.0 57.1 0.5
N04 B:VOV303 2.0 56.7 0.5
N03 B:VOV303 2.0 55.9 0.5
NC B:FEC302 2.1 57.1 0.4
NB B:FEC302 2.1 57.9 0.4
NE2 B:HIS174 2.7 71.1 1.0
C4D B:FEC302 2.8 59.5 0.4
C1A B:FEC302 2.9 55.8 0.4
C10 B:VOV303 3.0 59.7 0.5
C1D B:FEC302 3.0 57.9 0.4
C18 B:VOV303 3.0 56.0 0.5
C07 B:VOV303 3.0 58.5 0.5
C43 B:VOV303 3.0 55.9 0.5
C32 B:VOV303 3.0 58.0 0.5
C40 B:VOV303 3.0 57.3 0.5
C29 B:VOV303 3.1 57.0 0.5
C4A B:FEC302 3.1 55.0 0.4
C4C B:FEC302 3.1 55.9 0.4
C21 B:VOV303 3.1 55.1 0.5
C1C B:FEC302 3.1 57.6 0.4
C4B B:FEC302 3.2 58.1 0.4
C1B B:FEC302 3.2 56.9 0.4
CHA B:FEC302 3.2 58.1 0.4
HD2 B:HIS174 3.2 85.6 1.0
CD2 B:HIS174 3.3 71.3 1.0
C17 B:VOV303 3.3 58.1 0.5
C06 B:VOV303 3.4 55.1 0.5
CHD B:FEC302 3.4 55.2 0.4
C39 B:VOV303 3.4 57.4 0.5
C28 B:VOV303 3.4 55.2 0.5
CHC B:FEC302 3.5 57.4 0.4
CHB B:FEC302 3.5 55.2 0.4
HG13 B:ILE189 3.8 48.6 1.0
CE1 B:HIS174 3.8 71.3 1.0
HD11 B:ILE189 3.9 48.6 1.0
HHA B:FEC302 4.1 69.7 0.4
C3D B:FEC302 4.1 61.0 0.4
HE1 B:HIS174 4.1 85.6 1.0
C2D B:FEC302 4.1 60.9 0.4
C09 B:VOV303 4.2 61.7 0.5
C2A B:FEC302 4.2 55.6 0.4
HG3 B:GLN187 4.2 62.3 1.0
C08 B:VOV303 4.2 60.9 0.5
H171 B:VOV303 4.2 69.8 0.5
C3A B:FEC302 4.2 55.1 0.4
C19 B:VOV303 4.2 55.7 0.5
C42 B:VOV303 4.2 56.4 0.5
C31 B:VOV303 4.2 60.3 0.5
C41 B:VOV303 4.3 58.0 0.5
H391 B:VOV303 4.3 68.9 0.5
C30 B:VOV303 4.3 59.1 0.5
C20 B:VOV303 4.3 55.1 0.5
H061 B:VOV303 4.3 66.2 0.5
C3C B:FEC302 4.3 56.4 0.4
C2C B:FEC302 4.3 58.0 0.4
HHD B:FEC302 4.3 66.2 0.4
H281 B:VOV303 4.4 66.3 0.5
HHC B:FEC302 4.4 68.9 0.4
C3B B:FEC302 4.4 60.6 0.4
C2B B:FEC302 4.4 59.4 0.4
HHB B:FEC302 4.4 66.3 0.4
CD1 B:ILE189 4.5 40.5 1.0
HD12 B:ILE189 4.5 48.6 1.0
CG1 B:ILE189 4.5 40.5 1.0
CG B:HIS174 4.6 67.1 1.0
HE2 B:MET219 4.8 81.4 1.0
HE1 B:MET219 4.8 81.4 1.0
ND1 B:HIS174 4.8 70.2 1.0
HG12 B:ILE189 4.8 48.6 1.0

Iron binding site 5 out of 10 in 6fxq

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Iron binding site 5 out of 10 in the Structure of Coproheme Decarboxylase From Listeria Monocytogenes During Turnover


Mono view


Stereo pair view

A full contact list of Iron with other atoms in the Fe binding site number 5 of Structure of Coproheme Decarboxylase From Listeria Monocytogenes During Turnover within 5.0Å range:
probe atom residue distance (Å) B Occ
C:Fe301

b:62.1
occ:0.47
FE C:FEC301 0.0 62.1 0.5
FE C:VOV302 0.3 62.2 0.3
N02 C:VOV302 1.9 60.2 0.3
N05 C:VOV302 2.0 65.1 0.3
ND C:FEC301 2.0 60.1 0.5
NC C:FEC301 2.0 65.1 0.5
NA C:FEC301 2.0 61.8 0.5
N03 C:VOV302 2.0 61.8 0.3
N04 C:VOV302 2.1 63.2 0.3
NB C:FEC301 2.1 63.2 0.5
C4D C:FEC301 3.0 59.0 0.5
C07 C:VOV302 3.0 60.4 0.3
C10 C:VOV302 3.0 59.0 0.3
C43 C:VOV302 3.0 65.2 0.3
C1A C:FEC301 3.0 60.7 0.5
C1C C:FEC301 3.0 65.9 0.5
C40 C:VOV302 3.0 65.7 0.3
C4B C:FEC301 3.0 64.4 0.5
C1D C:FEC301 3.0 60.5 0.5
NE2 C:HIS174 3.0 61.6 1.0
C4C C:FEC301 3.1 65.2 0.5
C18 C:VOV302 3.1 60.7 0.3
C32 C:VOV302 3.1 64.4 0.3
C29 C:VOV302 3.1 64.0 0.3
C4A C:FEC301 3.1 61.4 0.5
C21 C:VOV302 3.1 61.4 0.3
C1B C:FEC301 3.1 63.7 0.5
HD2 C:HIS174 3.2 74.7 1.0
CHA C:FEC301 3.3 59.2 0.5
C06 C:VOV302 3.3 62.9 0.3
CHC C:FEC301 3.4 65.2 0.5
C17 C:VOV302 3.4 59.2 0.3
CHD C:FEC301 3.4 62.9 0.5
C39 C:VOV302 3.4 65.2 0.3
CD2 C:HIS174 3.5 62.2 1.0
C28 C:VOV302 3.5 62.6 0.3
CHB C:FEC301 3.5 62.5 0.5
HG13 C:ILE189 3.8 48.7 1.0
HD11 C:ILE189 4.0 49.4 1.0
C08 C:VOV302 4.2 60.1 0.3
C09 C:VOV302 4.2 60.1 0.3
C42 C:VOV302 4.2 65.5 0.3
HHA C:FEC301 4.2 71.0 0.5
C3D C:FEC301 4.2 60.2 0.5
C41 C:VOV302 4.2 66.0 0.3
C2C C:FEC301 4.2 66.0 0.5
C2D C:FEC301 4.2 60.2 0.5
C2A C:FEC301 4.3 60.5 0.5
C3C C:FEC301 4.3 65.6 0.5
H061 C:VOV302 4.3 75.5 0.3
HHC C:FEC301 4.3 78.3 0.5
C19 C:VOV302 4.3 60.6 0.3
C31 C:VOV302 4.3 65.4 0.3
H171 C:VOV302 4.3 71.1 0.3
CE1 C:HIS174 4.3 62.2 1.0
C3A C:FEC301 4.3 59.6 0.5
C3B C:FEC301 4.3 65.2 0.5
H391 C:VOV302 4.3 78.3 0.3
C30 C:VOV302 4.3 65.6 0.3
C20 C:VOV302 4.3 59.5 0.3
HG3 C:GLN187 4.3 75.5 1.0
HHD C:FEC301 4.4 75.5 0.5
C2B C:FEC301 4.4 65.6 0.5
H281 C:VOV302 4.4 75.1 0.3
HHB C:FEC301 4.4 75.1 0.5
HE1 C:MET219 4.4 85.8 1.0
CG1 C:ILE189 4.6 40.6 1.0
CD1 C:ILE189 4.6 41.1 1.0
HD12 C:ILE189 4.6 49.4 1.0
HE1 C:HIS174 4.7 74.6 1.0
HE2 C:MET219 4.8 85.8 1.0
CG C:HIS174 4.8 57.6 1.0
HG12 C:ILE189 4.9 48.7 1.0

Iron binding site 6 out of 10 in 6fxq

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Iron binding site 6 out of 10 in the Structure of Coproheme Decarboxylase From Listeria Monocytogenes During Turnover


Mono view


Stereo pair view

A full contact list of Iron with other atoms in the Fe binding site number 6 of Structure of Coproheme Decarboxylase From Listeria Monocytogenes During Turnover within 5.0Å range:
probe atom residue distance (Å) B Occ
C:Fe302

b:62.2
occ:0.34
FE C:VOV302 0.0 62.2 0.3
FE C:FEC301 0.3 62.1 0.5
N02 C:VOV302 2.0 60.2 0.3
N04 C:VOV302 2.0 63.2 0.3
N05 C:VOV302 2.0 65.1 0.3
N03 C:VOV302 2.0 61.8 0.3
NA C:FEC301 2.0 61.8 0.5
NB C:FEC301 2.0 63.2 0.5
NC C:FEC301 2.0 65.1 0.5
ND C:FEC301 2.1 60.1 0.5
NE2 C:HIS174 2.8 61.6 1.0
HD2 C:HIS174 2.9 74.7 1.0
C4B C:FEC301 3.0 64.4 0.5
C1A C:FEC301 3.0 60.7 0.5
C4D C:FEC301 3.0 59.0 0.5
C10 C:VOV302 3.0 59.0 0.3
C1C C:FEC301 3.0 65.9 0.5
C32 C:VOV302 3.0 64.4 0.3
C18 C:VOV302 3.0 60.7 0.3
C40 C:VOV302 3.1 65.7 0.3
C29 C:VOV302 3.1 64.0 0.3
C07 C:VOV302 3.1 60.4 0.3
C43 C:VOV302 3.1 65.2 0.3
C4A C:FEC301 3.1 61.4 0.5
C1B C:FEC301 3.1 63.7 0.5
C21 C:VOV302 3.1 61.4 0.3
C1D C:FEC301 3.2 60.5 0.5
C4C C:FEC301 3.2 65.2 0.5
CD2 C:HIS174 3.2 62.2 1.0
CHA C:FEC301 3.3 59.2 0.5
CHC C:FEC301 3.3 65.2 0.5
C17 C:VOV302 3.4 59.2 0.3
C39 C:VOV302 3.4 65.2 0.3
C28 C:VOV302 3.4 62.6 0.3
C06 C:VOV302 3.4 62.9 0.3
CHB C:FEC301 3.5 62.5 0.5
CHD C:FEC301 3.5 62.9 0.5
CE1 C:HIS174 4.1 62.2 1.0
HG13 C:ILE189 4.1 48.7 1.0
HHA C:FEC301 4.2 71.0 0.5
HHC C:FEC301 4.2 78.3 0.5
C09 C:VOV302 4.2 60.1 0.3
C31 C:VOV302 4.2 65.4 0.3
C08 C:VOV302 4.2 60.1 0.3
C2A C:FEC301 4.2 60.5 0.5
C3B C:FEC301 4.3 65.2 0.5
H391 C:VOV302 4.3 78.3 0.3
C19 C:VOV302 4.3 60.6 0.3
C30 C:VOV302 4.3 65.6 0.3
C3D C:FEC301 4.3 60.2 0.5
C41 C:VOV302 4.3 66.0 0.3
C3A C:FEC301 4.3 59.6 0.5
H171 C:VOV302 4.3 71.1 0.3
C2C C:FEC301 4.3 66.0 0.5
C42 C:VOV302 4.3 65.5 0.3
HD11 C:ILE189 4.3 49.4 1.0
C20 C:VOV302 4.3 59.5 0.3
C2B C:FEC301 4.3 65.6 0.5
C2D C:FEC301 4.3 60.2 0.5
C3C C:FEC301 4.3 65.6 0.5
HE1 C:MET219 4.4 85.8 1.0
H281 C:VOV302 4.4 75.1 0.3
H061 C:VOV302 4.4 75.5 0.3
HHB C:FEC301 4.4 75.1 0.5
HHD C:FEC301 4.5 75.5 0.5
CG C:HIS174 4.5 57.6 1.0
HE1 C:HIS174 4.5 74.6 1.0
HG3 C:GLN187 4.6 75.5 1.0
HE2 C:MET219 4.6 85.8 1.0
HA2 C:GLY175 4.8 57.3 1.0
HD12 C:ILE189 4.9 49.4 1.0
CD1 C:ILE189 4.9 41.1 1.0
CG1 C:ILE189 4.9 40.6 1.0
ND1 C:HIS174 4.9 61.3 1.0
CE C:MET219 4.9 71.5 1.0

Iron binding site 7 out of 10 in 6fxq

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Iron binding site 7 out of 10 in the Structure of Coproheme Decarboxylase From Listeria Monocytogenes During Turnover


Mono view


Stereo pair view

A full contact list of Iron with other atoms in the Fe binding site number 7 of Structure of Coproheme Decarboxylase From Listeria Monocytogenes During Turnover within 5.0Å range:
probe atom residue distance (Å) B Occ
D:Fe301

b:38.5
occ:0.62
FE D:FEC301 0.0 38.5 0.6
FE D:VOV302 0.2 39.0 0.3
N02 D:VOV302 1.9 37.0 0.3
ND D:FEC301 1.9 36.8 0.6
N05 D:VOV302 2.0 41.2 0.3
NC D:FEC301 2.0 41.3 0.6
N03 D:VOV302 2.0 36.2 0.3
NA D:FEC301 2.0 36.0 0.6
NB D:FEC301 2.1 41.7 0.6
N04 D:VOV302 2.1 41.8 0.3
NE2 D:HIS174 2.5 42.0 1.0
C10 D:VOV302 2.9 37.4 0.3
C07 D:VOV302 2.9 37.7 0.3
C4D D:FEC301 2.9 37.2 0.6
C43 D:VOV302 3.0 41.0 0.3
C18 D:VOV302 3.0 35.3 0.3
C1A D:FEC301 3.0 35.0 0.6
C1D D:FEC301 3.0 37.6 0.6
C1C D:FEC301 3.0 42.9 0.6
C4C D:FEC301 3.0 40.6 0.6
C4B D:FEC301 3.1 44.8 0.6
C40 D:VOV302 3.1 42.8 0.3
C4A D:FEC301 3.1 35.7 0.6
C1B D:FEC301 3.1 43.5 0.6
C21 D:VOV302 3.1 36.1 0.3
C32 D:VOV302 3.1 44.8 0.3
C29 D:VOV302 3.2 43.8 0.3
C17 D:VOV302 3.3 35.5 0.3
CHA D:FEC301 3.3 35.4 0.6
C06 D:VOV302 3.3 39.5 0.3
CD2 D:HIS174 3.4 42.6 1.0
CHC D:FEC301 3.4 43.9 0.6
HD2 D:HIS174 3.4 51.2 1.0
CHD D:FEC301 3.4 39.7 0.6
CHB D:FEC301 3.5 39.1 0.6
C39 D:VOV302 3.5 43.9 0.3
C28 D:VOV302 3.5 39.3 0.3
CE1 D:HIS174 3.6 42.1 1.0
HD11 D:ILE189 3.7 42.0 1.0
HG13 D:ILE189 3.8 40.3 1.0
HE1 D:HIS174 3.8 50.6 1.0
HG3 D:GLN187 4.0 51.6 1.0
C09 D:VOV302 4.1 41.6 0.3
C08 D:VOV302 4.1 39.0 0.3
H171 D:VOV302 4.1 42.7 0.3
C3D D:FEC301 4.2 41.6 0.6
C2D D:FEC301 4.2 39.6 0.6
HHA D:FEC301 4.2 42.5 0.6
C42 D:VOV302 4.2 41.5 0.3
HE1 D:MET219 4.2 51.6 1.0
C19 D:VOV302 4.2 34.7 0.3
C2C D:FEC301 4.2 43.8 0.6
C3C D:FEC301 4.3 41.5 0.6
H061 D:VOV302 4.3 47.5 0.3
C41 D:VOV302 4.3 44.1 0.3
C2A D:FEC301 4.3 34.3 0.6
HHC D:FEC301 4.3 52.7 0.6
C3A D:FEC301 4.3 35.1 0.6
C20 D:VOV302 4.3 35.2 0.3
C3B D:FEC301 4.3 50.3 0.6
HHD D:FEC301 4.3 47.7 0.6
H391 D:VOV302 4.3 52.7 0.3
CD1 D:ILE189 4.3 35.0 1.0
C31 D:VOV302 4.4 50.2 0.3
C2B D:FEC301 4.4 50.1 0.6
C30 D:VOV302 4.4 50.1 0.3
HHB D:FEC301 4.4 47.0 0.6
HD12 D:ILE189 4.4 42.0 1.0
H281 D:VOV302 4.4 47.2 0.3
CG1 D:ILE189 4.4 33.6 1.0
CG D:HIS174 4.6 39.5 1.0
HG12 D:ILE189 4.7 40.3 1.0
ND1 D:HIS174 4.7 42.1 1.0
HE2 D:MET219 4.8 51.6 1.0
HE21 D:GLN187 4.9 74.3 1.0
CE D:MET219 4.9 42.9 1.0
CG D:GLN187 5.0 43.0 1.0

Iron binding site 8 out of 10 in 6fxq

Go back to Iron Binding Sites List in 6fxq
Iron binding site 8 out of 10 in the Structure of Coproheme Decarboxylase From Listeria Monocytogenes During Turnover


Mono view


Stereo pair view

A full contact list of Iron with other atoms in the Fe binding site number 8 of Structure of Coproheme Decarboxylase From Listeria Monocytogenes During Turnover within 5.0Å range:
probe atom residue distance (Å) B Occ
D:Fe302

b:39.0
occ:0.29
FE D:VOV302 0.0 39.0 0.3
FE D:FEC301 0.2 38.5 0.6
NB D:FEC301 1.9 41.7 0.6
N02 D:VOV302 2.0 37.0 0.3
N04 D:VOV302 2.0 41.8 0.3
N05 D:VOV302 2.0 41.2 0.3
NC D:FEC301 2.0 41.3 0.6
N03 D:VOV302 2.0 36.2 0.3
NA D:FEC301 2.0 36.0 0.6
ND D:FEC301 2.1 36.8 0.6
NE2 D:HIS174 2.5 42.0 1.0
C4B D:FEC301 2.9 44.8 0.6
C1B D:FEC301 3.0 43.5 0.6
C1C D:FEC301 3.0 42.9 0.6
C10 D:VOV302 3.0 37.4 0.3
C4A D:FEC301 3.0 35.7 0.6
C32 D:VOV302 3.0 44.8 0.3
C18 D:VOV302 3.0 35.3 0.3
C40 D:VOV302 3.0 42.8 0.3
C1A D:FEC301 3.1 35.0 0.6
C29 D:VOV302 3.1 43.8 0.3
C43 D:VOV302 3.1 41.0 0.3
C4D D:FEC301 3.1 37.2 0.6
C07 D:VOV302 3.1 37.7 0.3
C21 D:VOV302 3.1 36.1 0.3
C4C D:FEC301 3.1 40.6 0.6
C1D D:FEC301 3.2 37.6 0.6
CD2 D:HIS174 3.3 42.6 1.0
HD2 D:HIS174 3.3 51.2 1.0
CHC D:FEC301 3.3 43.9 0.6
C17 D:VOV302 3.4 35.5 0.3
CHB D:FEC301 3.4 39.1 0.6
CHA D:FEC301 3.4 35.4 0.6
C39 D:VOV302 3.4 43.9 0.3
C28 D:VOV302 3.4 39.3 0.3
C06 D:VOV302 3.4 39.5 0.3
CHD D:FEC301 3.5 39.7 0.6
CE1 D:HIS174 3.6 42.1 1.0
HD11 D:ILE189 3.8 42.0 1.0
HG13 D:ILE189 3.8 40.3 1.0
HE1 D:HIS174 3.8 50.6 1.0
HG3 D:GLN187 4.1 51.6 1.0
HHC D:FEC301 4.2 52.7 0.6
C3B D:FEC301 4.2 50.3 0.6
H171 D:VOV302 4.2 42.7 0.3
C09 D:VOV302 4.2 41.6 0.3
C2B D:FEC301 4.2 50.1 0.6
C31 D:VOV302 4.2 50.2 0.3
H391 D:VOV302 4.2 52.7 0.3
C2C D:FEC301 4.2 43.8 0.6
C08 D:VOV302 4.2 39.0 0.3
C19 D:VOV302 4.3 34.7 0.3
C3A D:FEC301 4.3 35.1 0.6
C42 D:VOV302 4.3 41.5 0.3
C30 D:VOV302 4.3 50.1 0.3
C41 D:VOV302 4.3 44.1 0.3
C2A D:FEC301 4.3 34.3 0.6
C20 D:VOV302 4.3 35.2 0.3
HHA D:FEC301 4.3 42.5 0.6
HE1 D:MET219 4.3 51.6 1.0
C3C D:FEC301 4.3 41.5 0.6
C3D D:FEC301 4.3 41.6 0.6
HHB D:FEC301 4.3 47.0 0.6
C2D D:FEC301 4.3 39.6 0.6
H281 D:VOV302 4.4 47.2 0.3
H061 D:VOV302 4.4 47.5 0.3
HHD D:FEC301 4.5 47.7 0.6
CD1 D:ILE189 4.5 35.0 1.0
CG D:HIS174 4.5 39.5 1.0
CG1 D:ILE189 4.5 33.6 1.0
HD12 D:ILE189 4.5 42.0 1.0
ND1 D:HIS174 4.6 42.1 1.0
HG12 D:ILE189 4.7 40.3 1.0
HE2 D:MET219 4.8 51.6 1.0
HE21 D:GLN187 4.9 74.3 1.0
CE D:MET219 5.0 42.9 1.0

Iron binding site 9 out of 10 in 6fxq

Go back to Iron Binding Sites List in 6fxq
Iron binding site 9 out of 10 in the Structure of Coproheme Decarboxylase From Listeria Monocytogenes During Turnover


Mono view


Stereo pair view

A full contact list of Iron with other atoms in the Fe binding site number 9 of Structure of Coproheme Decarboxylase From Listeria Monocytogenes During Turnover within 5.0Å range:
probe atom residue distance (Å) B Occ
E:Fe301

b:55.8
occ:0.44
FE E:FEC301 0.0 55.8 0.4
FE E:VOV302 0.1 55.9 0.4
N04 E:VOV302 2.0 58.9 0.4
ND E:FEC301 2.0 56.0 0.4
N03 E:VOV302 2.0 56.6 0.4
NC E:FEC301 2.0 56.5 0.4
NA E:FEC301 2.0 56.6 0.4
N02 E:VOV302 2.0 56.0 0.4
N05 E:VOV302 2.0 56.5 0.4
NB E:FEC301 2.1 59.4 0.4
NE2 E:HIS174 2.6 55.2 1.0
C4D E:FEC301 2.9 57.0 0.4
C1A E:FEC301 3.0 56.4 0.4
C29 E:VOV302 3.0 60.2 0.4
C18 E:VOV302 3.0 56.4 0.4
C1C E:FEC301 3.0 57.5 0.4
C32 E:VOV302 3.0 60.6 0.4
C10 E:VOV302 3.0 57.0 0.4
C21 E:VOV302 3.0 56.6 0.4
C4B E:FEC301 3.0 60.8 0.4
C1D E:FEC301 3.0 56.3 0.4
C4C E:FEC301 3.1 56.4 0.4
C40 E:VOV302 3.1 57.2 0.4
C07 E:VOV302 3.1 56.8 0.4
C43 E:VOV302 3.1 56.2 0.4
C4A E:FEC301 3.1 56.6 0.4
C1B E:FEC301 3.1 60.0 0.4
CHA E:FEC301 3.3 56.8 0.4
CHC E:FEC301 3.3 58.6 0.4
C17 E:VOV302 3.3 56.8 0.4
HD2 E:HIS174 3.4 66.9 1.0
C28 E:VOV302 3.4 58.0 0.4
CD2 E:HIS174 3.4 55.8 1.0
C39 E:VOV302 3.4 58.6 0.4
CHD E:FEC301 3.4 55.9 0.4
C06 E:VOV302 3.5 55.9 0.4
CHB E:FEC301 3.5 58.0 0.4
HG13 E:ILE189 3.7 39.2 1.0
CE1 E:HIS174 3.7 55.4 1.0
HE1 E:HIS174 4.0 66.5 1.0
HD11 E:ILE189 4.0 39.4 1.0
HG3 E:GLN187 4.2 76.7 1.0
HHA E:FEC301 4.2 68.2 0.4
C30 E:VOV302 4.2 62.5 0.4
H171 E:VOV302 4.2 68.2 0.4
C3D E:FEC301 4.2 58.3 0.4
C19 E:VOV302 4.2 56.0 0.4
C31 E:VOV302 4.2 64.1 0.4
HE1 E:MET219 4.2 51.9 1.0
C2A E:FEC301 4.2 55.9 0.4
C20 E:VOV302 4.2 56.0 0.4
C2D E:FEC301 4.2 57.2 0.4
C09 E:VOV302 4.2 58.6 0.4
HHC E:FEC301 4.2 70.4 0.4
C2C E:FEC301 4.2 58.9 0.4
H391 E:VOV302 4.2 70.3 0.4
C08 E:VOV302 4.3 57.2 0.4
C3C E:FEC301 4.3 56.7 0.4
C3A E:FEC301 4.3 56.0 0.4
C41 E:VOV302 4.3 58.6 0.4
H281 E:VOV302 4.3 69.7 0.4
C42 E:VOV302 4.3 56.6 0.4
C3B E:FEC301 4.3 64.1 0.4
HHD E:FEC301 4.3 67.1 0.4
C2B E:FEC301 4.4 63.2 0.4
H061 E:VOV302 4.4 67.2 0.4
HHB E:FEC301 4.4 69.7 0.4
CG1 E:ILE189 4.4 32.6 1.0
HE21 E:GLN187 4.5 87.1 1.0
CD1 E:ILE189 4.6 32.8 1.0
CG E:HIS174 4.6 54.5 1.0
HD12 E:ILE189 4.6 39.4 1.0
HG12 E:ILE189 4.7 39.2 1.0
ND1 E:HIS174 4.8 55.0 1.0
HE2 E:MET219 4.9 51.9 1.0
HA2 E:GLY175 5.0 58.3 1.0
CE E:MET219 5.0 43.2 1.0

Iron binding site 10 out of 10 in 6fxq

Go back to Iron Binding Sites List in 6fxq
Iron binding site 10 out of 10 in the Structure of Coproheme Decarboxylase From Listeria Monocytogenes During Turnover


Mono view


Stereo pair view

A full contact list of Iron with other atoms in the Fe binding site number 10 of Structure of Coproheme Decarboxylase From Listeria Monocytogenes During Turnover within 5.0Å range:
probe atom residue distance (Å) B Occ
E:Fe302

b:55.9
occ:0.43
FE E:VOV302 0.0 55.9 0.4
FE E:FEC301 0.1 55.8 0.4
ND E:FEC301 1.9 56.0 0.4
NC E:FEC301 2.0 56.5 0.4
N02 E:VOV302 2.0 56.0 0.4
N04 E:VOV302 2.0 58.9 0.4
N05 E:VOV302 2.0 56.5 0.4
N03 E:VOV302 2.0 56.6 0.4
NA E:FEC301 2.1 56.6 0.4
NB E:FEC301 2.1 59.4 0.4
NE2 E:HIS174 2.5 55.2 1.0
C4D E:FEC301 2.9 57.0 0.4
C10 E:VOV302 3.0 57.0 0.4
C1A E:FEC301 3.0 56.4 0.4
C1D E:FEC301 3.0 56.3 0.4
C1C E:FEC301 3.0 57.5 0.4
C18 E:VOV302 3.0 56.4 0.4
C4C E:FEC301 3.0 56.4 0.4
C32 E:VOV302 3.0 60.6 0.4
C29 E:VOV302 3.0 60.2 0.4
C07 E:VOV302 3.0 56.8 0.4
C4B E:FEC301 3.1 60.8 0.4
C40 E:VOV302 3.1 57.2 0.4
C43 E:VOV302 3.1 56.2 0.4
C21 E:VOV302 3.1 56.6 0.4
C4A E:FEC301 3.1 56.6 0.4
C1B E:FEC301 3.2 60.0 0.4
CHA E:FEC301 3.3 56.8 0.4
HD2 E:HIS174 3.3 66.9 1.0
CD2 E:HIS174 3.3 55.8 1.0
C17 E:VOV302 3.3 56.8 0.4
CHC E:FEC301 3.3 58.6 0.4
CHD E:FEC301 3.4 55.9 0.4
C39 E:VOV302 3.4 58.6 0.4
C06 E:VOV302 3.4 55.9 0.4
C28 E:VOV302 3.4 58.0 0.4
CHB E:FEC301 3.6 58.0 0.4
CE1 E:HIS174 3.6 55.4 1.0
HG13 E:ILE189 3.8 39.2 1.0
HE1 E:HIS174 3.9 66.5 1.0
HD11 E:ILE189 4.1 39.4 1.0
HE1 E:MET219 4.1 51.9 1.0
HHA E:FEC301 4.2 68.2 0.4
C3D E:FEC301 4.2 58.3 0.4
H171 E:VOV302 4.2 68.2 0.4
C2D E:FEC301 4.2 57.2 0.4
C09 E:VOV302 4.2 58.6 0.4
C08 E:VOV302 4.2 57.2 0.4
C2C E:FEC301 4.2 58.9 0.4
H391 E:VOV302 4.2 70.3 0.4
HHC E:FEC301 4.2 70.4 0.4
C19 E:VOV302 4.2 56.0 0.4
C31 E:VOV302 4.2 64.1 0.4
C3C E:FEC301 4.2 56.7 0.4
C30 E:VOV302 4.2 62.5 0.4
HG3 E:GLN187 4.2 76.7 1.0
C2A E:FEC301 4.2 55.9 0.4
C41 E:VOV302 4.3 58.6 0.4
C42 E:VOV302 4.3 56.6 0.4
C20 E:VOV302 4.3 56.0 0.4
C3A E:FEC301 4.3 56.0 0.4
HHD E:FEC301 4.3 67.1 0.4
C3B E:FEC301 4.3 64.1 0.4
H061 E:VOV302 4.3 67.2 0.4
H281 E:VOV302 4.4 69.7 0.4
C2B E:FEC301 4.4 63.2 0.4
HHB E:FEC301 4.5 69.7 0.4
CG E:HIS174 4.5 54.5 1.0
HE21 E:GLN187 4.5 87.1 1.0
CG1 E:ILE189 4.6 32.6 1.0
CD1 E:ILE189 4.6 32.8 1.0
ND1 E:HIS174 4.6 55.0 1.0
HD12 E:ILE189 4.7 39.4 1.0
HG12 E:ILE189 4.8 39.2 1.0
HE2 E:MET219 4.8 51.9 1.0
CE E:MET219 4.9 43.2 1.0
HA2 E:GLY175 4.9 58.3 1.0

Reference:

L.Milazzo, T.Gabler, D.Puhringer, Z.Jandova, D.Maresch, H.Michlits, V.Pfanzagl, K.Djinovic-Carugo, C.Oostenbrink, P.G.Furtmuller, C.Obinger, G.Smulevich, S.Hofbauer. Redox Cofactor Rotates During Its Stepwise Decarboxylation: Molecular Mechanism of Conversion of Coproheme to Hemeb. Acs Catalysis V. 9 6766 2019.
ISSN: ESSN 2155-5435
PubMed: 31423350
DOI: 10.1021/ACSCATAL.9B00963
Page generated: Tue Aug 6 18:45:58 2024

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