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Iron in PDB 9ctz: Azotobacter Vinelandii Mofep (C2 Symmetry)

Enzymatic activity of Azotobacter Vinelandii Mofep (C2 Symmetry)

All present enzymatic activity of Azotobacter Vinelandii Mofep (C2 Symmetry):
1.18.6.1;

Other elements in 9ctz:

The structure of Azotobacter Vinelandii Mofep (C2 Symmetry) also contains other interesting chemical elements:

Molybdenum (Mo) 2 atoms

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 Azotobacter Vinelandii Mofep (C2 Symmetry) (pdb code 9ctz). This binding sites where shown within 5.0 Angstroms radius around Iron atom.
In total 32 binding sites of Iron where determined in the Azotobacter Vinelandii Mofep (C2 Symmetry), PDB code: 9ctz:
Jump to Iron binding site number: 1; 2; 3; 4; 5; 6; 7; 8; 9; 10;

Iron binding site 1 out of 32 in 9ctz

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Iron binding site 1 out of 32 in the Azotobacter Vinelandii Mofep (C2 Symmetry)


Mono view


Stereo pair view

A full contact list of Iron with other atoms in the Fe binding site number 1 of Azotobacter Vinelandii Mofep (C2 Symmetry) within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Fe502

b:104.7
occ:1.00
FE1 A:ICS502 0.0 104.7 1.0
S2A A:ICS502 2.3 82.7 1.0
S4A A:ICS502 2.3 69.2 1.0
S1A A:ICS502 2.3 75.0 1.0
SG A:CYS275 2.3 74.3 1.0
FE4 A:ICS502 2.6 87.4 1.0
FE3 A:ICS502 2.6 102.5 1.0
FE2 A:ICS502 2.7 83.6 1.0
CX A:ICS502 3.4 87.3 1.0
CB A:CYS275 3.5 61.9 1.0
CB A:LEU358 4.1 75.5 1.0
OG A:SER278 4.3 66.8 1.0
CB A:SER278 4.5 57.9 1.0
CE2 A:TYR229 4.6 56.6 1.0
CA A:CYS275 4.7 60.4 1.0
N A:LEU358 4.7 78.6 1.0
S3A A:ICS502 4.8 77.6 1.0
S5A A:ICS502 4.8 69.3 1.0
S2B A:ICS502 4.8 83.2 1.0
CD2 A:LEU358 4.8 72.5 1.0
FE7 A:ICS502 5.0 90.4 1.0
FE5 A:ICS502 5.0 100.3 1.0
FE6 A:ICS502 5.0 88.1 1.0
N A:SER278 5.0 65.0 1.0

Iron binding site 2 out of 32 in 9ctz

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Iron binding site 2 out of 32 in the Azotobacter Vinelandii Mofep (C2 Symmetry)


Mono view


Stereo pair view

A full contact list of Iron with other atoms in the Fe binding site number 2 of Azotobacter Vinelandii Mofep (C2 Symmetry) within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Fe502

b:83.6
occ:1.00
FE2 A:ICS502 0.0 83.6 1.0
CX A:ICS502 2.0 87.3 1.0
S2B A:ICS502 2.2 83.2 1.0
S2A A:ICS502 2.2 82.7 1.0
S1A A:ICS502 2.3 75.0 1.0
FE6 A:ICS502 2.6 88.1 1.0
FE4 A:ICS502 2.7 87.4 1.0
FE3 A:ICS502 2.7 102.5 1.0
FE1 A:ICS502 2.7 104.7 1.0
FE5 A:ICS502 3.7 100.3 1.0
FE7 A:ICS502 3.7 90.4 1.0
S4A A:ICS502 3.9 69.2 1.0
CE1 A:HIS195 4.0 51.1 1.0
CZ A:PHE381 4.0 71.1 1.0
S1B A:ICS502 4.2 78.1 1.0
S3B A:ICS502 4.2 78.1 1.0
NE2 A:HIS195 4.3 54.3 1.0
CE1 A:PHE381 4.4 71.3 1.0
S3A A:ICS502 4.5 77.6 1.0
S5A A:ICS502 4.5 69.3 1.0
CG1 A:VAL70 4.6 43.7 1.0
SG A:CYS275 4.8 74.3 1.0
N A:GLY357 4.9 71.3 1.0
CG2 A:VAL70 4.9 48.1 1.0
MO1 A:ICS502 5.0 105.5 1.0

Iron binding site 3 out of 32 in 9ctz

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Iron binding site 3 out of 32 in the Azotobacter Vinelandii Mofep (C2 Symmetry)


Mono view


Stereo pair view

A full contact list of Iron with other atoms in the Fe binding site number 3 of Azotobacter Vinelandii Mofep (C2 Symmetry) within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Fe502

b:102.5
occ:1.00
FE3 A:ICS502 0.0 102.5 1.0
CX A:ICS502 2.0 87.3 1.0
S5A A:ICS502 2.2 69.3 1.0
S4A A:ICS502 2.2 69.2 1.0
S2A A:ICS502 2.3 82.7 1.0
FE7 A:ICS502 2.6 90.4 1.0
FE4 A:ICS502 2.6 87.4 1.0
FE1 A:ICS502 2.6 104.7 1.0
FE2 A:ICS502 2.7 83.6 1.0
FE6 A:ICS502 3.7 88.1 1.0
FE5 A:ICS502 3.7 100.3 1.0
S1A A:ICS502 3.8 75.0 1.0
NH2 A:ARG96 4.2 61.8 1.0
CD2 A:TYR229 4.2 56.3 1.0
S4B A:ICS502 4.2 84.6 1.0
S3B A:ICS502 4.2 78.1 1.0
CE2 A:TYR229 4.3 56.6 1.0
S2B A:ICS502 4.4 83.2 1.0
S3A A:ICS502 4.5 77.6 1.0
SG A:CYS275 4.7 74.3 1.0
NE A:ARG359 5.0 74.0 1.0
MO1 A:ICS502 5.0 105.5 1.0

Iron binding site 4 out of 32 in 9ctz

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Iron binding site 4 out of 32 in the Azotobacter Vinelandii Mofep (C2 Symmetry)


Mono view


Stereo pair view

A full contact list of Iron with other atoms in the Fe binding site number 4 of Azotobacter Vinelandii Mofep (C2 Symmetry) within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Fe502

b:87.4
occ:1.00
FE4 A:ICS502 0.0 87.4 1.0
CX A:ICS502 2.0 87.3 1.0
S3A A:ICS502 2.2 77.6 1.0
S4A A:ICS502 2.3 69.2 1.0
S1A A:ICS502 2.3 75.0 1.0
FE5 A:ICS502 2.6 100.3 1.0
FE1 A:ICS502 2.6 104.7 1.0
FE3 A:ICS502 2.6 102.5 1.0
FE2 A:ICS502 2.7 83.6 1.0
FE7 A:ICS502 3.7 90.4 1.0
FE6 A:ICS502 3.7 88.1 1.0
N A:LEU358 3.8 78.6 1.0
S2A A:ICS502 3.8 82.7 1.0
N A:GLY357 3.9 71.3 1.0
CB A:LEU358 4.1 75.5 1.0
S4B A:ICS502 4.2 84.6 1.0
S1B A:ICS502 4.3 78.1 1.0
S5A A:ICS502 4.5 69.3 1.0
N A:ARG359 4.5 76.4 1.0
CA A:LEU358 4.5 80.7 1.0
CA A:GLY357 4.5 73.7 1.0
S2B A:ICS502 4.5 83.2 1.0
C A:GLY357 4.6 79.0 1.0
SG A:CYS275 4.6 74.3 1.0
C A:GLY356 4.9 75.2 1.0
NE A:ARG359 4.9 74.0 1.0

Iron binding site 5 out of 32 in 9ctz

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Iron binding site 5 out of 32 in the Azotobacter Vinelandii Mofep (C2 Symmetry)


Mono view


Stereo pair view

A full contact list of Iron with other atoms in the Fe binding site number 5 of Azotobacter Vinelandii Mofep (C2 Symmetry) within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Fe502

b:100.3
occ:1.00
FE5 A:ICS502 0.0 100.3 1.0
CX A:ICS502 2.0 87.3 1.0
S4B A:ICS502 2.2 84.6 1.0
S3A A:ICS502 2.3 77.6 1.0
S1B A:ICS502 2.3 78.1 1.0
FE4 A:ICS502 2.6 87.4 1.0
FE7 A:ICS502 2.6 90.4 1.0
FE6 A:ICS502 2.6 88.1 1.0
MO1 A:ICS502 2.7 105.5 1.0
FE2 A:ICS502 3.7 83.6 1.0
FE3 A:ICS502 3.7 102.5 1.0
S3B A:ICS502 3.9 78.1 1.0
CG2 A:ILE355 4.1 73.8 1.0
ND1 A:HIS442 4.2 69.0 1.0
S1A A:ICS502 4.3 75.0 1.0
N A:GLY356 4.3 76.5 1.0
S4A A:ICS502 4.3 69.2 1.0
CA A:GLY356 4.4 75.4 1.0
S5A A:ICS502 4.5 69.3 1.0
S2B A:ICS502 4.5 83.2 1.0
CD A:ARG359 4.6 73.0 1.0
N A:GLY357 4.7 71.3 1.0
CE1 A:HIS442 4.7 72.6 1.0
NE A:ARG359 4.8 74.0 1.0
NH1 A:ARG359 4.9 68.4 1.0
FE1 A:ICS502 5.0 104.7 1.0

Iron binding site 6 out of 32 in 9ctz

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Iron binding site 6 out of 32 in the Azotobacter Vinelandii Mofep (C2 Symmetry)


Mono view


Stereo pair view

A full contact list of Iron with other atoms in the Fe binding site number 6 of Azotobacter Vinelandii Mofep (C2 Symmetry) within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Fe502

b:88.1
occ:1.00
FE6 A:ICS502 0.0 88.1 1.0
CX A:ICS502 2.0 87.3 1.0
S2B A:ICS502 2.2 83.2 1.0
S3B A:ICS502 2.2 78.1 1.0
S1B A:ICS502 2.2 78.1 1.0
FE2 A:ICS502 2.6 83.6 1.0
FE7 A:ICS502 2.6 90.4 1.0
MO1 A:ICS502 2.6 105.5 1.0
FE5 A:ICS502 2.6 100.3 1.0
FE3 A:ICS502 3.7 102.5 1.0
FE4 A:ICS502 3.7 87.4 1.0
S4B A:ICS502 3.8 84.6 1.0
O7 A:HCA501 3.9 67.7 1.0
CZ A:PHE381 4.2 71.1 1.0
S2A A:ICS502 4.2 82.7 1.0
S1A A:ICS502 4.3 75.0 1.0
O1 A:HCA501 4.4 71.8 1.0
S5A A:ICS502 4.5 69.3 1.0
CG2 A:VAL70 4.5 48.1 1.0
S3A A:ICS502 4.5 77.6 1.0
CE2 A:PHE381 4.8 68.0 1.0
O5 A:HCA501 4.9 75.3 1.0
FE1 A:ICS502 5.0 104.7 1.0

Iron binding site 7 out of 32 in 9ctz

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Iron binding site 7 out of 32 in the Azotobacter Vinelandii Mofep (C2 Symmetry)


Mono view


Stereo pair view

A full contact list of Iron with other atoms in the Fe binding site number 7 of Azotobacter Vinelandii Mofep (C2 Symmetry) within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Fe502

b:90.4
occ:1.00
FE7 A:ICS502 0.0 90.4 1.0
CX A:ICS502 2.0 87.3 1.0
S5A A:ICS502 2.2 69.3 1.0
S4B A:ICS502 2.2 84.6 1.0
S3B A:ICS502 2.2 78.1 1.0
FE3 A:ICS502 2.6 102.5 1.0
FE6 A:ICS502 2.6 88.1 1.0
FE5 A:ICS502 2.6 100.3 1.0
MO1 A:ICS502 2.6 105.5 1.0
FE2 A:ICS502 3.7 83.6 1.0
FE4 A:ICS502 3.7 87.4 1.0
S1B A:ICS502 3.8 78.1 1.0
NE A:ARG96 4.2 61.5 1.0
NH2 A:ARG96 4.2 61.8 1.0
O A:HOH688 4.2 62.0 1.0
S2A A:ICS502 4.3 82.7 1.0
S4A A:ICS502 4.3 69.2 1.0
S2B A:ICS502 4.4 83.2 1.0
NH1 A:ARG359 4.4 68.4 1.0
O5 A:HCA501 4.4 75.3 1.0
CZ A:ARG359 4.5 70.3 1.0
S3A A:ICS502 4.5 77.6 1.0
CZ A:ARG96 4.7 57.4 1.0
NH2 A:ARG359 4.8 66.7 1.0
NE A:ARG359 4.8 74.0 1.0
O7 A:HCA501 4.9 67.7 1.0
FE1 A:ICS502 5.0 104.7 1.0

Iron binding site 8 out of 32 in 9ctz

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Iron binding site 8 out of 32 in the Azotobacter Vinelandii Mofep (C2 Symmetry)


Mono view


Stereo pair view

A full contact list of Iron with other atoms in the Fe binding site number 8 of Azotobacter Vinelandii Mofep (C2 Symmetry) within 5.0Å range:
probe atom residue distance (Å) B Occ
B:Fe601

b:77.2
occ:1.00
OD2 B:ASP353 2.1 67.2 1.0
OE2 D:GLU109 2.2 64.3 1.0
O D:ARG108 2.4 59.1 1.0
OD2 B:ASP357 2.5 57.8 1.0
CG B:ASP353 3.1 60.4 1.0
CD D:GLU109 3.3 62.4 1.0
OD1 B:ASP353 3.4 69.8 1.0
CG B:ASP357 3.4 54.5 1.0
C D:ARG108 3.5 53.3 1.0
OD1 B:ASP357 3.7 59.1 1.0
CG D:GLU109 3.7 57.8 1.0
CB D:ARG108 4.2 49.3 1.0
OE1 D:GLU109 4.3 59.4 1.0
N D:GLU109 4.4 50.7 1.0
CA D:GLU109 4.4 49.9 1.0
CB B:ASP353 4.4 46.5 1.0
O D:HOH790 4.5 63.3 1.0
CA D:ARG108 4.5 45.5 1.0
O B:ASP353 4.5 47.1 1.0
O D:PHE107 4.6 46.2 1.0
O D:HOH763 4.6 51.9 1.0
CB D:GLU109 4.6 52.9 1.0
NZ C:LYS433 4.7 61.4 1.0
CD1 C:PHE429 4.7 58.7 1.0
O B:HOH719 4.7 62.5 1.0
CB B:ASP357 4.8 49.3 1.0
CE C:LYS433 4.8 61.3 1.0
C B:ASP353 4.9 44.4 1.0

Iron binding site 9 out of 32 in 9ctz

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Iron binding site 9 out of 32 in the Azotobacter Vinelandii Mofep (C2 Symmetry)


Mono view


Stereo pair view

A full contact list of Iron with other atoms in the Fe binding site number 9 of Azotobacter Vinelandii Mofep (C2 Symmetry) within 5.0Å range:
probe atom residue distance (Å) B Occ
B:Fe602

b:63.6
occ:1.00
FE1 B:CLF602 0.0 63.6 1.0
SG B:CYS95 2.1 52.3 1.0
S3A B:CLF602 2.3 56.1 1.0
S2A B:CLF602 2.3 47.2 1.0
FE4 B:CLF602 2.5 62.4 1.0
S1 B:CLF602 2.5 62.2 1.0
FE2 B:CLF602 2.5 64.3 1.0
FE3 B:CLF602 2.7 66.3 1.0
FE8 B:CLF602 3.1 64.6 1.0
N B:CYS95 3.3 40.1 1.0
CB B:CYS95 3.5 41.8 1.0
CA B:CYS95 3.6 36.4 1.0
S4A B:CLF602 3.8 46.9 1.0
C B:GLY94 3.9 43.0 1.0
S4B B:CLF602 4.3 51.8 1.0
CA B:GLY94 4.5 37.8 1.0
O B:GLY94 4.6 49.0 1.0
FE5 B:CLF602 4.6 82.5 1.0
SG A:CYS154 4.6 46.6 1.0
CB B:SER92 4.7 50.5 1.0
SG A:CYS62 4.7 55.8 1.0
N B:GLY94 4.8 41.5 1.0
OG B:SER92 5.0 52.4 1.0
SG A:CYS88 5.0 53.3 1.0

Iron binding site 10 out of 32 in 9ctz

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Iron binding site 10 out of 32 in the Azotobacter Vinelandii Mofep (C2 Symmetry)


Mono view


Stereo pair view

A full contact list of Iron with other atoms in the Fe binding site number 10 of Azotobacter Vinelandii Mofep (C2 Symmetry) within 5.0Å range:
probe atom residue distance (Å) B Occ
B:Fe602

b:64.3
occ:1.00
FE2 B:CLF602 0.0 64.3 1.0
S2A B:CLF602 2.3 47.2 1.0
S4A B:CLF602 2.3 46.9 1.0
SG A:CYS154 2.3 46.6 1.0
S1 B:CLF602 2.4 62.2 1.0
FE1 B:CLF602 2.5 63.6 1.0
FE4 B:CLF602 2.6 62.4 1.0
FE3 B:CLF602 2.8 66.3 1.0
CB A:CYS154 3.5 40.6 1.0
S3A B:CLF602 3.8 56.1 1.0
SG B:CYS95 4.0 52.3 1.0
CA A:GLY185 4.1 48.7 1.0
N A:CYS154 4.1 44.9 1.0
N A:GLY185 4.3 48.7 1.0
FE8 B:CLF602 4.4 64.6 1.0
CA A:CYS154 4.4 43.4 1.0
OG B:SER92 4.5 52.4 1.0
SG B:CYS153 4.7 61.4 1.0
CB B:SER92 4.7 50.5 1.0
C A:GLY185 4.8 49.4 1.0
SG A:CYS88 4.9 53.3 1.0

Reference:

S.M.Narehood, B.D.Cook, S.Srisantitham, V.H.Eng, A.Shiau, K.L.Mcguire, R.D.Britt, M.A.Herzik, F.A.Tezcan. Structural Basis For the Conformational Protection of Nitrogenase From O2 Nature 2025.
ISSN: ESSN 1476-4687
DOI: 10.1038/S41586-024-08311-1
Page generated: Sat Feb 8 18:53:44 2025

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