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Iron in PDB 6bbl: Crystal Structure of the A-96GLN Mofe Protein Variant in the Presence of the Substrate Acetylene

Enzymatic activity of Crystal Structure of the A-96GLN Mofe Protein Variant in the Presence of the Substrate Acetylene

All present enzymatic activity of Crystal Structure of the A-96GLN Mofe Protein Variant in the Presence of the Substrate Acetylene:
1.18.6.1;

Protein crystallography data

The structure of Crystal Structure of the A-96GLN Mofe Protein Variant in the Presence of the Substrate Acetylene, PDB code: 6bbl was solved by O.A.Zadvornyy, S.M.Keable, J.Vertemara, B.J.Eilers, D.Karamatullah, A.J.Rasmussen, L.De Gioia, G.Zampella, L.C.Seefeldt, J.W.Peters, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 39.76 / 1.68
Space group P 1 21 1
Cell size a, b, c (Å), α, β, γ (°) 76.781, 128.251, 107.272, 90.00, 109.11, 90.00
R / Rfree (%) 15.1 / 18.5

Other elements in 6bbl:

The structure of Crystal Structure of the A-96GLN Mofe Protein Variant in the Presence of the Substrate Acetylene also contains other interesting chemical elements:

Molybdenum (Mo) 2 atoms
Magnesium (Mg) 1 atom

Iron Binding Sites:

Pages:

>>> Page 1 <<< Page 2, Binding sites: 11 - 20; Page 3, Binding sites: 21 - 30; Page 4, Binding sites: 31 - 32;

Binding sites:

The binding sites of Iron atom in the Crystal Structure of the A-96GLN Mofe Protein Variant in the Presence of the Substrate Acetylene (pdb code 6bbl). This binding sites where shown within 5.0 Angstroms radius around Iron atom.
In total 32 binding sites of Iron where determined in the Crystal Structure of the A-96GLN Mofe Protein Variant in the Presence of the Substrate Acetylene, PDB code: 6bbl:
Jump to Iron binding site number: 1; 2; 3; 4; 5; 6; 7; 8; 9; 10;

Iron binding site 1 out of 32 in 6bbl

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Iron binding site 1 out of 32 in the Crystal Structure of the A-96GLN Mofe Protein Variant in the Presence of the Substrate Acetylene


Mono view


Stereo pair view

A full contact list of Iron with other atoms in the Fe binding site number 1 of Crystal Structure of the A-96GLN Mofe Protein Variant in the Presence of the Substrate Acetylene within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Fe504

b:18.4
occ:1.00
FE1 A:ICS504 0.0 18.4 1.0
S2A A:ICS504 2.1 15.3 0.8
S4A A:ICS504 2.2 16.9 0.9
S1A A:ICS504 2.2 17.8 1.0
SG A:CYS275 2.3 17.4 1.0
FE4 A:ICS504 2.6 17.9 1.0
FE3 A:ICS504 2.7 17.0 1.0
FE2 A:ICS504 2.7 17.1 1.0
HB2 A:CYS275 3.1 22.2 1.0
CB A:CYS275 3.3 18.5 1.0
CX A:ICS504 3.4 10.6 1.0
HG A:SER278 3.6 21.8 1.0
HB2 A:LEU358 3.7 22.1 1.0
HE2 A:TYR229 3.7 24.5 1.0
HB3 A:SER278 3.7 23.6 1.0
HB3 A:LEU358 3.7 22.1 1.0
HB3 A:CYS275 3.7 22.2 1.0
HD22 A:LEU358 3.9 28.2 1.0
OG A:SER278 4.1 18.2 1.0
CB A:LEU358 4.2 18.4 1.0
HB3 A:ARG277 4.3 23.3 1.0
H A:SER278 4.3 25.1 1.0
HD2 A:TYR229 4.4 22.4 1.0
CB A:SER278 4.4 19.6 1.0
CE2 A:TYR229 4.4 20.4 1.0
HA A:CYS275 4.4 22.8 1.0
CA A:CYS275 4.5 19.0 1.0
CD2 A:LEU358 4.7 23.5 1.0
HD23 A:LEU358 4.7 28.2 1.0
S3A A:ICS504 4.8 17.6 1.0
CD2 A:TYR229 4.8 18.7 1.0
S2B A:ICS504 4.8 18.2 1.0
S5A A:ICS504 4.8 19.6 1.0
HE1 A:HIS195 4.8 25.4 1.0
H A:GLY357 4.9 23.7 1.0
FE5 A:ICS504 5.0 17.6 1.0
N A:SER278 5.0 21.0 1.0
FE6 A:ICS504 5.0 17.6 1.0
FE7 A:ICS504 5.0 17.3 1.0
N A:LEU358 5.0 20.8 1.0

Iron binding site 2 out of 32 in 6bbl

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Iron binding site 2 out of 32 in the Crystal Structure of the A-96GLN Mofe Protein Variant in the Presence of the Substrate Acetylene


Mono view


Stereo pair view

A full contact list of Iron with other atoms in the Fe binding site number 2 of Crystal Structure of the A-96GLN Mofe Protein Variant in the Presence of the Substrate Acetylene within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Fe504

b:17.1
occ:1.00
FE2 A:ICS504 0.0 17.1 1.0
CX A:ICS504 1.9 10.6 1.0
S1A A:ICS504 2.1 17.8 1.0
S2A A:ICS504 2.1 15.3 0.8
S2B A:ICS504 2.2 18.2 1.0
FE6 A:ICS504 2.5 17.6 1.0
FE4 A:ICS504 2.5 17.9 1.0
FE3 A:ICS504 2.5 17.0 1.0
FE1 A:ICS504 2.7 18.4 1.0
HZ A:PHE381 3.1 22.7 1.0
FE5 A:ICS504 3.6 17.6 1.0
S4A A:ICS504 3.6 16.9 0.9
FE7 A:ICS504 3.6 17.3 1.0
HE2 A:HIS195 3.6 20.6 1.0
HE1 A:HIS195 3.6 25.4 1.0
HG11 A:VAL70 3.7 33.8 1.0
CZ A:PHE381 4.0 18.9 1.0
S1B A:ICS504 4.0 17.2 1.0
S3B A:ICS504 4.1 16.9 1.0
NE2 A:HIS195 4.1 17.2 1.0
CE1 A:HIS195 4.1 21.1 1.0
HG21 A:VAL70 4.1 30.3 1.0
HE1 A:PHE381 4.2 21.7 1.0
HB3 A:SER278 4.2 23.6 1.0
S3A A:ICS504 4.4 17.6 1.0
S5A A:ICS504 4.5 19.6 1.0
H A:GLY357 4.5 23.7 1.0
CE1 A:PHE381 4.5 18.1 1.0
CG1 A:VAL70 4.6 28.2 1.0
SG A:CYS275 4.7 17.4 1.0
HA3 A:GLY356 4.8 22.1 1.0
HA3 A:GLY357 4.9 27.3 1.0
MO1 A:ICS504 5.0 19.0 1.0
HG12 A:VAL70 5.0 33.8 1.0
CG2 A:VAL70 5.0 25.3 1.0

Iron binding site 3 out of 32 in 6bbl

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Iron binding site 3 out of 32 in the Crystal Structure of the A-96GLN Mofe Protein Variant in the Presence of the Substrate Acetylene


Mono view


Stereo pair view

A full contact list of Iron with other atoms in the Fe binding site number 3 of Crystal Structure of the A-96GLN Mofe Protein Variant in the Presence of the Substrate Acetylene within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Fe504

b:17.0
occ:1.00
FE3 A:ICS504 0.0 17.0 1.0
CX A:ICS504 1.9 10.6 1.0
S4A A:ICS504 2.1 16.9 0.9
S2A A:ICS504 2.1 15.3 0.8
S5A A:ICS504 2.2 19.6 1.0
FE4 A:ICS504 2.5 17.9 1.0
FE7 A:ICS504 2.5 17.3 1.0
FE2 A:ICS504 2.5 17.1 1.0
FE1 A:ICS504 2.7 18.4 1.0
HD2 A:TYR229 3.4 22.4 1.0
FE6 A:ICS504 3.6 17.6 1.0
S1A A:ICS504 3.6 17.8 1.0
FE5 A:ICS504 3.6 17.6 1.0
HG11 A:VAL70 3.8 33.8 1.0
CD2 A:TYR229 4.0 18.7 1.0
S3B A:ICS504 4.1 16.9 1.0
S4B A:ICS504 4.1 16.4 0.9
HE2 A:TYR229 4.2 24.5 1.0
O A:HOH909 4.2 19.2 1.0
S2B A:ICS504 4.4 18.2 1.0
HG12 A:VAL70 4.4 33.8 1.0
CE2 A:TYR229 4.4 20.4 1.0
S3A A:ICS504 4.5 17.6 1.0
CG1 A:VAL70 4.6 28.2 1.0
HB2 A:TYR229 4.6 22.5 1.0
HB2 A:CYS275 4.7 22.2 1.0
SG A:CYS275 4.9 17.4 1.0
CG A:TYR229 4.9 18.6 1.0
HB A:VAL70 5.0 31.7 1.0
MO1 A:ICS504 5.0 19.0 1.0

Iron binding site 4 out of 32 in 6bbl

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Iron binding site 4 out of 32 in the Crystal Structure of the A-96GLN Mofe Protein Variant in the Presence of the Substrate Acetylene


Mono view


Stereo pair view

A full contact list of Iron with other atoms in the Fe binding site number 4 of Crystal Structure of the A-96GLN Mofe Protein Variant in the Presence of the Substrate Acetylene within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Fe504

b:17.9
occ:1.00
FE4 A:ICS504 0.0 17.9 1.0
CX A:ICS504 1.9 10.6 1.0
S1A A:ICS504 2.1 17.8 1.0
S4A A:ICS504 2.1 16.9 0.9
S3A A:ICS504 2.3 17.6 1.0
FE2 A:ICS504 2.5 17.1 1.0
FE5 A:ICS504 2.5 17.6 1.0
FE3 A:ICS504 2.5 17.0 1.0
FE1 A:ICS504 2.6 18.4 1.0
H A:GLY357 3.3 23.7 1.0
HB3 A:LEU358 3.4 22.1 1.0
S2A A:ICS504 3.6 15.3 0.8
FE6 A:ICS504 3.6 17.6 1.0
FE7 A:ICS504 3.6 17.3 1.0
H A:LEU358 3.6 24.9 1.0
H A:ARG359 4.0 21.2 1.0
HG3 A:ARG359 4.0 19.5 1.0
N A:GLY357 4.0 19.8 1.0
N A:LEU358 4.1 20.8 1.0
S1B A:ICS504 4.1 17.2 1.0
S4B A:ICS504 4.1 16.4 0.9
HB2 A:LEU358 4.1 22.1 1.0
HZ A:PHE381 4.1 22.7 1.0
CB A:LEU358 4.1 18.4 1.0
HA3 A:GLY356 4.2 22.1 1.0
S5A A:ICS504 4.4 19.6 1.0
S2B A:ICS504 4.5 18.2 1.0
HD2 A:ARG359 4.5 21.7 1.0
HA3 A:GLY357 4.5 27.3 1.0
H A:GLY356 4.6 25.0 1.0
CA A:GLY357 4.6 22.7 1.0
C A:GLY357 4.6 23.4 1.0
SG A:CYS275 4.6 17.4 1.0
CA A:LEU358 4.7 20.2 1.0
N A:ARG359 4.8 17.7 1.0
CG A:ARG359 4.9 16.2 1.0
HD23 A:LEU358 4.9 28.2 1.0
HD22 A:LEU358 4.9 28.2 1.0
CA A:GLY356 4.9 18.5 1.0
CZ A:PHE381 4.9 18.9 1.0
C A:GLY356 5.0 17.5 1.0
MO1 A:ICS504 5.0 19.0 1.0

Iron binding site 5 out of 32 in 6bbl

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Iron binding site 5 out of 32 in the Crystal Structure of the A-96GLN Mofe Protein Variant in the Presence of the Substrate Acetylene


Mono view


Stereo pair view

A full contact list of Iron with other atoms in the Fe binding site number 5 of Crystal Structure of the A-96GLN Mofe Protein Variant in the Presence of the Substrate Acetylene within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Fe504

b:17.6
occ:1.00
FE5 A:ICS504 0.0 17.6 1.0
CX A:ICS504 2.0 10.6 1.0
S4B A:ICS504 2.1 16.4 0.9
S1B A:ICS504 2.1 17.2 1.0
S3A A:ICS504 2.3 17.6 1.0
FE4 A:ICS504 2.5 17.9 1.0
FE6 A:ICS504 2.6 17.6 1.0
FE7 A:ICS504 2.6 17.3 1.0
MO1 A:ICS504 2.7 19.0 1.0
HA3 A:GLY356 3.4 22.1 1.0
HG22 A:ILE355 3.5 23.4 1.0
FE2 A:ICS504 3.6 17.1 1.0
FE3 A:ICS504 3.6 17.0 1.0
H A:GLY356 3.6 25.0 1.0
S3B A:ICS504 3.7 16.9 1.0
ND1 A:HIS442 3.8 22.8 1.0
HD2 A:ARG359 3.9 21.7 1.0
H A:GLY357 4.0 23.7 1.0
S1A A:ICS504 4.1 17.8 1.0
S4A A:ICS504 4.1 16.9 0.9
N A:GLY356 4.2 20.8 1.0
CA A:GLY356 4.2 18.5 1.0
HZ A:PHE381 4.2 22.7 1.0
HE1 A:HIS442 4.2 24.1 1.0
HG21 A:ILE355 4.3 23.4 1.0
CG2 A:ILE355 4.3 19.5 1.0
CE1 A:HIS442 4.3 20.1 1.0
S5A A:ICS504 4.5 19.6 1.0
S2B A:ICS504 4.5 18.2 1.0
O7 A:HCA503 4.6 19.4 1.0
HA A:HIS442 4.6 19.8 1.0
N A:GLY357 4.7 19.8 1.0
CG A:HIS442 4.7 15.6 1.0
HG3 A:ARG359 4.7 19.5 1.0
HB3 A:HIS442 4.7 23.0 1.0
O6 A:HCA503 4.8 19.0 1.0
CD A:ARG359 4.8 18.1 1.0
HA2 A:GLY356 4.8 22.1 1.0
HG23 A:ILE355 4.9 23.4 1.0
H A:LEU358 4.9 24.9 1.0
FE1 A:ICS504 5.0 18.4 1.0
HB2 A:ARG359 5.0 20.8 1.0
H A:ARG359 5.0 21.2 1.0
HH11 A:ARG359 5.0 24.2 1.0
CZ A:PHE381 5.0 18.9 1.0
C A:GLY356 5.0 17.5 1.0

Iron binding site 6 out of 32 in 6bbl

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Iron binding site 6 out of 32 in the Crystal Structure of the A-96GLN Mofe Protein Variant in the Presence of the Substrate Acetylene


Mono view


Stereo pair view

A full contact list of Iron with other atoms in the Fe binding site number 6 of Crystal Structure of the A-96GLN Mofe Protein Variant in the Presence of the Substrate Acetylene within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Fe504

b:17.6
occ:1.00
FE6 A:ICS504 0.0 17.6 1.0
CX A:ICS504 2.0 10.6 1.0
S1B A:ICS504 2.1 17.2 1.0
S3B A:ICS504 2.1 16.9 1.0
S2B A:ICS504 2.2 18.2 1.0
FE2 A:ICS504 2.5 17.1 1.0
FE7 A:ICS504 2.5 17.3 1.0
FE5 A:ICS504 2.6 17.6 1.0
MO1 A:ICS504 2.7 19.0 1.0
HZ A:PHE381 3.3 22.7 1.0
FE3 A:ICS504 3.6 17.0 1.0
FE4 A:ICS504 3.6 17.9 1.0
S4B A:ICS504 3.6 16.4 0.9
HG11 A:VAL70 3.7 33.8 1.0
O7 A:HCA503 3.8 19.4 1.0
H2 A:C2H501 4.1 36.8 1.0
S1A A:ICS504 4.1 17.8 1.0
CZ A:PHE381 4.1 18.9 1.0
S2A A:ICS504 4.1 15.3 0.8
C A:C2H501 4.2 30.7 1.0
HA3 A:GLY356 4.2 22.1 1.0
HE2 A:PHE381 4.2 22.6 1.0
S5A A:ICS504 4.4 19.6 1.0
C1 A:C2H501 4.5 22.6 1.0
S3A A:ICS504 4.5 17.6 1.0
O2 A:HCA503 4.5 23.3 1.0
O6 A:HCA503 4.5 19.0 1.0
CG1 A:VAL70 4.6 28.2 1.0
CE2 A:PHE381 4.6 18.9 1.0
HE2 A:HIS195 4.7 20.6 1.0
HG13 A:VAL70 4.7 33.8 1.0
H22 A:HCA503 4.7 24.1 1.0
ND1 A:HIS442 4.8 22.8 1.0
C3 A:HCA503 4.8 22.7 1.0
HG12 A:VAL70 4.9 33.8 1.0
FE1 A:ICS504 5.0 18.4 1.0
HE1 A:HIS442 5.0 24.1 1.0
HE21 A:GLN191 5.0 28.6 1.0

Iron binding site 7 out of 32 in 6bbl

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Iron binding site 7 out of 32 in the Crystal Structure of the A-96GLN Mofe Protein Variant in the Presence of the Substrate Acetylene


Mono view


Stereo pair view

A full contact list of Iron with other atoms in the Fe binding site number 7 of Crystal Structure of the A-96GLN Mofe Protein Variant in the Presence of the Substrate Acetylene within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Fe504

b:17.3
occ:1.00
FE7 A:ICS504 0.0 17.3 1.0
CX A:ICS504 2.0 10.6 1.0
S3B A:ICS504 2.1 16.9 1.0
S4B A:ICS504 2.1 16.4 0.9
S5A A:ICS504 2.2 19.6 1.0
FE3 A:ICS504 2.5 17.0 1.0
FE6 A:ICS504 2.5 17.6 1.0
FE5 A:ICS504 2.6 17.6 1.0
MO1 A:ICS504 2.7 19.0 1.0
FE4 A:ICS504 3.6 17.9 1.0
FE2 A:ICS504 3.6 17.1 1.0
S1B A:ICS504 3.6 17.2 1.0
O6 A:HCA503 3.8 19.0 1.0
O A:HOH811 3.8 20.1 1.0
HG11 A:VAL70 4.0 33.8 1.0
O A:HOH767 4.1 25.9 1.0
S4A A:ICS504 4.1 16.9 0.9
S2A A:ICS504 4.2 15.3 0.8
HG12 A:VAL70 4.3 33.8 1.0
S2B A:ICS504 4.4 18.2 1.0
HB3 A:HIS442 4.4 23.0 1.0
S3A A:ICS504 4.5 17.6 1.0
CG1 A:VAL70 4.6 28.2 1.0
O7 A:HCA503 4.7 19.4 1.0
HG13 A:ILE231 4.7 22.0 1.0
C7 A:HCA503 4.7 21.4 1.0
HD11 A:ILE231 4.8 23.1 1.0
HA A:HIS442 4.8 19.8 1.0
ND1 A:HIS442 4.8 22.8 1.0
NH1 A:ARG359 4.8 20.2 1.0
CZ A:ARG359 4.9 21.6 1.0
HD2 A:ARG359 4.9 21.7 1.0
HH12 A:ARG359 4.9 24.2 1.0
HG13 A:VAL70 4.9 33.8 1.0
FE1 A:ICS504 5.0 18.4 1.0

Iron binding site 8 out of 32 in 6bbl

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Iron binding site 8 out of 32 in the Crystal Structure of the A-96GLN Mofe Protein Variant in the Presence of the Substrate Acetylene


Mono view


Stereo pair view

A full contact list of Iron with other atoms in the Fe binding site number 8 of Crystal Structure of the A-96GLN Mofe Protein Variant in the Presence of the Substrate Acetylene within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Fe505

b:18.1
occ:1.00
FE1 A:1CL505 0.0 18.1 1.0
S2A A:1CL505 2.2 16.0 1.0
S3A A:1CL505 2.2 17.1 1.0
FE4 A:1CL505 2.3 18.5 1.0
S1 A:1CL505 2.3 16.7 1.0
FE2 A:1CL505 2.3 15.7 0.9
FE3 A:1CL505 2.4 17.2 1.0
SG A:CYS88 2.7 15.9 1.0
FE5 A:1CL505 3.2 26.8 1.0
HB3 A:CYS88 3.3 22.9 1.0
S4A A:1CL505 3.3 17.3 1.0
CB A:CYS88 3.6 19.1 1.0
HB3 A:GLU153 3.8 18.2 1.0
FE8 A:1CL505 3.9 18.6 1.0
H A:CYS154 4.0 23.5 1.0
S4B A:1CL505 4.3 14.5 1.0
HB2 A:CYS88 4.3 22.9 1.0
HG2 A:GLU153 4.3 21.9 1.0
HB3 A:TYR64 4.4 22.0 1.0
HA A:CYS88 4.4 20.9 1.0
SG B:CYS95 4.5 18.3 1.0
HA3 A:GLY185 4.5 22.6 1.0
HE2 B:TYR98 4.6 22.5 1.0
HA A:GLU153 4.6 23.9 1.0
CA A:CYS88 4.6 17.4 1.0
SG A:CYS62 4.6 18.5 1.0
SG A:CYS154 4.7 20.1 1.0
CB A:GLU153 4.7 15.2 1.0
HD2 B:TYR98 4.7 20.1 1.0
N A:CYS154 4.8 19.6 1.0
H A:GLY185 4.8 25.2 1.0
HD1 A:TYR64 4.9 21.4 1.0
HB2 A:CYS154 4.9 25.3 1.0
H A:CYS88 4.9 22.1 1.0
HA B:CYS95 4.9 19.9 1.0
CG A:GLU153 4.9 18.3 1.0
CD1 A:TYR64 5.0 17.9 1.0
HB2 A:TYR64 5.0 22.0 1.0

Iron binding site 9 out of 32 in 6bbl

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Iron binding site 9 out of 32 in the Crystal Structure of the A-96GLN Mofe Protein Variant in the Presence of the Substrate Acetylene


Mono view


Stereo pair view

A full contact list of Iron with other atoms in the Fe binding site number 9 of Crystal Structure of the A-96GLN Mofe Protein Variant in the Presence of the Substrate Acetylene within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Fe505

b:15.7
occ:0.91
FE2 A:1CL505 0.0 15.7 0.9
S4A A:1CL505 2.1 17.3 1.0
S2A A:1CL505 2.2 16.0 1.0
FE1 A:1CL505 2.3 18.1 1.0
SG A:CYS154 2.4 20.1 1.0
S1 A:1CL505 2.4 16.7 1.0
FE4 A:1CL505 2.4 18.5 1.0
FE3 A:1CL505 2.7 17.2 1.0
HA3 A:GLY185 3.0 22.6 1.0
H A:CYS154 3.1 23.5 1.0
HB2 A:CYS154 3.4 25.3 1.0
H A:GLY185 3.5 25.2 1.0
CB A:CYS154 3.5 21.1 1.0
S3A A:1CL505 3.7 17.1 1.0
HG B:SER92 3.8 38.9 1.0
O B:HOH998 3.8 22.0 1.0
N A:CYS154 3.9 19.6 1.0
CA A:GLY185 3.9 18.9 1.0
HB2 B:SER92 4.0 28.4 1.0
N A:GLY185 4.1 21.0 1.0
CA A:CYS154 4.2 18.5 1.0
SG B:CYS95 4.3 18.3 1.0
HB3 A:CYS154 4.3 25.3 1.0
HA A:CYS154 4.4 22.2 1.0
HB3 A:GLU153 4.4 18.2 1.0
FE8 A:1CL505 4.4 18.6 1.0
HB3 B:SER92 4.5 28.4 1.0
OG B:SER92 4.5 32.4 1.0
HA2 A:GLY185 4.5 22.6 1.0
CB B:SER92 4.5 23.6 1.0
FE5 A:1CL505 4.7 26.8 1.0
C A:GLY185 4.7 21.0 1.0
HA A:GLU153 4.7 23.9 1.0
SG A:CYS88 4.7 15.9 1.0
H A:PHE186 4.9 27.0 1.0
SG A:CYS62 4.9 18.5 1.0
C A:GLU153 5.0 19.8 1.0

Iron binding site 10 out of 32 in 6bbl

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Iron binding site 10 out of 32 in the Crystal Structure of the A-96GLN Mofe Protein Variant in the Presence of the Substrate Acetylene


Mono view


Stereo pair view

A full contact list of Iron with other atoms in the Fe binding site number 10 of Crystal Structure of the A-96GLN Mofe Protein Variant in the Presence of the Substrate Acetylene within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Fe505

b:17.2
occ:1.00
FE3 A:1CL505 0.0 17.2 1.0
S4A A:1CL505 2.2 17.3 1.0
S3A A:1CL505 2.2 17.1 1.0
S2A A:1CL505 2.2 16.0 1.0
FE1 A:1CL505 2.4 18.1 1.0
SG A:CYS62 2.4 18.5 1.0
FE4 A:1CL505 2.7 18.5 1.0
FE2 A:1CL505 2.7 15.7 0.9
HA3 A:GLY185 3.1 22.6 1.0
HB3 A:TYR64 3.2 22.0 1.0
CB A:CYS62 3.4 16.2 1.0
HB3 A:CYS62 3.4 19.4 1.0
HB2 A:CYS62 3.5 19.4 1.0
HA3 B:GLY94 3.5 22.4 1.0
CA A:GLY185 3.9 18.9 1.0
HA2 A:GLY185 3.9 22.6 1.0
S1 A:1CL505 4.1 16.7 1.0
CB A:TYR64 4.2 18.4 1.0
H A:GLY185 4.2 25.2 1.0
HD1 A:TYR64 4.2 21.4 1.0
H A:TYR64 4.3 20.9 1.0
CA B:GLY94 4.3 18.7 1.0
HB2 A:TYR64 4.3 22.0 1.0
HE2 B:TYR98 4.5 22.5 1.0
C B:GLY94 4.5 16.9 1.0
N A:GLY185 4.5 21.0 1.0
H B:CYS95 4.6 22.0 1.0
HB3 A:CYS88 4.6 22.9 1.0
N B:CYS95 4.6 18.3 1.0
CD1 A:TYR64 4.7 17.9 1.0
O B:HOH1116 4.7 21.0 1.0
CG A:TYR64 4.7 17.0 1.0
H A:ALA65 4.7 23.3 1.0
H B:GLY94 4.8 21.1 1.0
CA A:CYS62 4.8 19.1 1.0
SG A:CYS154 4.8 20.1 1.0
SG A:CYS88 4.9 15.9 1.0
HA2 B:GLY94 5.0 22.4 1.0
N A:TYR64 5.0 17.4 1.0

Reference:

S.M.Keable, J.Vertemara, O.A.Zadvornyy, B.J.Eilers, K.Danyal, A.J.Rasmussen, L.De Gioia, G.Zampella, L.C.Seefeldt, J.W.Peters. Structural Characterization of the Nitrogenase Molybdenum-Iron Protein with the Substrate Acetylene Trapped Near the Active Site. J. Inorg. Biochem. V. 180 129 2017.
ISSN: ISSN 1873-3344
PubMed: 29275221
DOI: 10.1016/J.JINORGBIO.2017.12.008
Page generated: Sun Dec 13 16:21:22 2020

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