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Iron in PDB 9cqy: Azotobacter Vinelandii Oxidized Mofep (C2 Symmetry) Obtained Using the Spt Labtech Chameleon

Enzymatic activity of Azotobacter Vinelandii Oxidized Mofep (C2 Symmetry) Obtained Using the Spt Labtech Chameleon

All present enzymatic activity of Azotobacter Vinelandii Oxidized Mofep (C2 Symmetry) Obtained Using the Spt Labtech Chameleon:
1.18.6.1;

Other elements in 9cqy:

The structure of Azotobacter Vinelandii Oxidized Mofep (C2 Symmetry) Obtained Using the Spt Labtech Chameleon 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 Oxidized Mofep (C2 Symmetry) Obtained Using the Spt Labtech Chameleon (pdb code 9cqy). 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 Oxidized Mofep (C2 Symmetry) Obtained Using the Spt Labtech Chameleon, PDB code: 9cqy:
Jump to Iron binding site number: 1; 2; 3; 4; 5; 6; 7; 8; 9; 10;

Iron binding site 1 out of 32 in 9cqy

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Iron binding site 1 out of 32 in the Azotobacter Vinelandii Oxidized Mofep (C2 Symmetry) Obtained Using the Spt Labtech Chameleon


Mono view


Stereo pair view

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

b:67.6
occ:1.00
FE1 A:ICS502 0.0 67.6 1.0
SG A:CYS275 2.2 51.8 1.0
S2A A:ICS502 2.3 47.9 1.0
S4A A:ICS502 2.3 44.9 1.0
S1A A:ICS502 2.3 48.1 1.0
FE4 A:ICS502 2.7 61.1 1.0
FE3 A:ICS502 2.7 61.5 1.0
FE2 A:ICS502 2.7 57.6 1.0
CB A:CYS275 3.2 39.0 1.0
CX A:ICS502 3.4 56.9 1.0
OG A:SER278 4.0 49.3 1.0
CB A:LEU358 4.1 47.8 1.0
CB A:SER278 4.4 35.5 1.0
CA A:CYS275 4.5 40.4 1.0
CE2 A:TYR229 4.6 38.5 1.0
CD2 A:LEU358 4.7 46.5 1.0
N A:LEU358 4.8 53.4 1.0
S2B A:ICS502 4.8 47.2 1.0
S5A A:ICS502 4.8 51.6 1.0
S3A A:ICS502 4.8 45.1 1.0
N A:SER278 4.9 43.1 1.0
FE7 A:ICS502 5.0 62.4 1.0
FE6 A:ICS502 5.0 57.6 1.0

Iron binding site 2 out of 32 in 9cqy

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Iron binding site 2 out of 32 in the Azotobacter Vinelandii Oxidized Mofep (C2 Symmetry) Obtained Using the Spt Labtech Chameleon


Mono view


Stereo pair view

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

b:57.6
occ:1.00
FE2 A:ICS502 0.0 57.6 1.0
CX A:ICS502 2.0 56.9 1.0
S2B A:ICS502 2.2 47.2 1.0
S2A A:ICS502 2.2 47.9 1.0
S1A A:ICS502 2.3 48.1 1.0
FE6 A:ICS502 2.6 57.6 1.0
FE4 A:ICS502 2.7 61.1 1.0
FE1 A:ICS502 2.7 67.6 1.0
FE3 A:ICS502 2.7 61.5 1.0
FE5 A:ICS502 3.7 62.3 1.0
FE7 A:ICS502 3.7 62.4 1.0
NE2 A:HIS195 3.8 38.7 1.0
S4A A:ICS502 3.9 44.9 1.0
CZ A:PHE381 4.0 49.2 1.0
S3B A:ICS502 4.2 50.3 1.0
S1B A:ICS502 4.2 59.0 1.0
CE1 A:HIS195 4.3 36.9 1.0
S3A A:ICS502 4.5 45.1 1.0
CE1 A:PHE381 4.5 47.1 1.0
S5A A:ICS502 4.5 51.6 1.0
CG1 A:VAL70 4.5 31.6 1.0
SG A:CYS275 4.6 51.8 1.0
CD2 A:HIS195 4.9 36.9 1.0
N A:GLY357 4.9 51.9 1.0
CG2 A:VAL70 4.9 35.2 1.0
O A:HOH623 5.0 53.0 1.0

Iron binding site 3 out of 32 in 9cqy

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Iron binding site 3 out of 32 in the Azotobacter Vinelandii Oxidized Mofep (C2 Symmetry) Obtained Using the Spt Labtech Chameleon


Mono view


Stereo pair view

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

b:61.5
occ:1.00
FE3 A:ICS502 0.0 61.5 1.0
CX A:ICS502 2.0 56.9 1.0
S5A A:ICS502 2.2 51.6 1.0
S4A A:ICS502 2.2 44.9 1.0
S2A A:ICS502 2.3 47.9 1.0
FE7 A:ICS502 2.6 62.4 1.0
FE4 A:ICS502 2.6 61.1 1.0
FE1 A:ICS502 2.7 67.6 1.0
FE2 A:ICS502 2.7 57.6 1.0
O A:HOH755 3.2 58.2 1.0
FE6 A:ICS502 3.7 57.6 1.0
FE5 A:ICS502 3.7 62.3 1.0
S1A A:ICS502 3.9 48.1 1.0
NH2 A:ARG96 4.0 42.5 1.0
S3B A:ICS502 4.2 50.3 1.0
S4B A:ICS502 4.2 48.4 1.0
CD2 A:TYR229 4.2 37.8 1.0
O A:HOH780 4.4 44.6 1.0
CE2 A:TYR229 4.4 38.5 1.0
S2B A:ICS502 4.5 47.2 1.0
S3A A:ICS502 4.5 45.1 1.0
SG A:CYS275 4.8 51.8 1.0
NE A:ARG359 4.8 51.9 1.0
O A:HOH668 4.9 65.6 1.0
NH2 A:ARG359 5.0 45.5 1.0

Iron binding site 4 out of 32 in 9cqy

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Iron binding site 4 out of 32 in the Azotobacter Vinelandii Oxidized Mofep (C2 Symmetry) Obtained Using the Spt Labtech Chameleon


Mono view


Stereo pair view

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

b:61.1
occ:1.00
FE4 A:ICS502 0.0 61.1 1.0
CX A:ICS502 2.0 56.9 1.0
S3A A:ICS502 2.2 45.1 1.0
S4A A:ICS502 2.3 44.9 1.0
S1A A:ICS502 2.3 48.1 1.0
FE5 A:ICS502 2.6 62.3 1.0
FE3 A:ICS502 2.6 61.5 1.0
FE1 A:ICS502 2.7 67.6 1.0
FE2 A:ICS502 2.7 57.6 1.0
FE7 A:ICS502 3.7 62.4 1.0
FE6 A:ICS502 3.7 57.6 1.0
N A:LEU358 3.7 53.4 1.0
S2A A:ICS502 3.8 47.9 1.0
N A:GLY357 3.9 51.9 1.0
CB A:LEU358 4.0 47.8 1.0
S4B A:ICS502 4.2 48.4 1.0
S1B A:ICS502 4.3 59.0 1.0
CA A:LEU358 4.4 52.1 1.0
S5A A:ICS502 4.5 51.6 1.0
S2B A:ICS502 4.5 47.2 1.0
CG A:ARG359 4.5 47.5 1.0
CA A:GLY357 4.5 50.0 1.0
C A:GLY357 4.5 57.5 1.0
N A:ARG359 4.6 55.4 1.0
SG A:CYS275 4.6 51.8 1.0
CD A:ARG359 4.7 50.3 1.0
NE A:ARG359 4.7 51.9 1.0
O A:HOH755 4.9 58.2 1.0
C A:GLY356 4.9 51.3 1.0
CZ A:PHE381 4.9 49.2 1.0

Iron binding site 5 out of 32 in 9cqy

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Iron binding site 5 out of 32 in the Azotobacter Vinelandii Oxidized Mofep (C2 Symmetry) Obtained Using the Spt Labtech Chameleon


Mono view


Stereo pair view

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

b:62.3
occ:1.00
FE5 A:ICS502 0.0 62.3 1.0
CX A:ICS502 2.0 56.9 1.0
S4B A:ICS502 2.2 48.4 1.0
S3A A:ICS502 2.3 45.1 1.0
S1B A:ICS502 2.3 59.0 1.0
FE4 A:ICS502 2.6 61.1 1.0
FE7 A:ICS502 2.6 62.4 1.0
FE6 A:ICS502 2.6 57.6 1.0
MO1 A:ICS502 2.7 72.5 1.0
FE2 A:ICS502 3.7 57.6 1.0
FE3 A:ICS502 3.7 61.5 1.0
S3B A:ICS502 3.9 50.3 1.0
N A:GLY356 4.2 49.6 1.0
CA A:GLY356 4.2 49.6 1.0
O A:HOH755 4.2 58.2 1.0
ND1 A:HIS442 4.2 50.1 1.0
S1A A:ICS502 4.3 48.1 1.0
S4A A:ICS502 4.3 44.9 1.0
CG2 A:ILE355 4.4 53.0 1.0
CD A:ARG359 4.4 50.3 1.0
S2B A:ICS502 4.4 47.2 1.0
S5A A:ICS502 4.5 51.6 1.0
N A:GLY357 4.5 51.9 1.0
NE A:ARG359 4.6 51.9 1.0
CE1 A:HIS442 4.6 52.8 1.0
CG A:ARG359 4.9 47.5 1.0
C A:GLY356 4.9 51.3 1.0
CZ A:PHE381 4.9 49.2 1.0

Iron binding site 6 out of 32 in 9cqy

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Iron binding site 6 out of 32 in the Azotobacter Vinelandii Oxidized Mofep (C2 Symmetry) Obtained Using the Spt Labtech Chameleon


Mono view


Stereo pair view

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

b:57.6
occ:1.00
FE6 A:ICS502 0.0 57.6 1.0
CX A:ICS502 2.0 56.9 1.0
S2B A:ICS502 2.2 47.2 1.0
S3B A:ICS502 2.2 50.3 1.0
S1B A:ICS502 2.2 59.0 1.0
FE2 A:ICS502 2.6 57.6 1.0
FE7 A:ICS502 2.6 62.4 1.0
FE5 A:ICS502 2.6 62.3 1.0
MO1 A:ICS502 2.7 72.5 1.0
FE3 A:ICS502 3.7 61.5 1.0
FE4 A:ICS502 3.7 61.1 1.0
S4B A:ICS502 3.8 48.4 1.0
CZ A:PHE381 4.1 49.2 1.0
O7 A:HCA501 4.2 52.8 1.0
S2A A:ICS502 4.2 47.9 1.0
O1 A:HCA501 4.3 48.8 1.0
S1A A:ICS502 4.3 48.1 1.0
CG2 A:VAL70 4.4 35.2 1.0
S5A A:ICS502 4.5 51.6 1.0
S3A A:ICS502 4.5 45.1 1.0
O A:HOH755 4.6 58.2 1.0
CE2 A:PHE381 4.6 48.0 1.0
O5 A:HCA501 4.9 48.6 1.0
FE1 A:ICS502 5.0 67.6 1.0

Iron binding site 7 out of 32 in 9cqy

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Iron binding site 7 out of 32 in the Azotobacter Vinelandii Oxidized Mofep (C2 Symmetry) Obtained Using the Spt Labtech Chameleon


Mono view


Stereo pair view

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

b:62.4
occ:1.00
FE7 A:ICS502 0.0 62.4 1.0
O A:HOH755 2.0 58.2 1.0
CX A:ICS502 2.0 56.9 1.0
S5A A:ICS502 2.2 51.6 1.0
S4B A:ICS502 2.2 48.4 1.0
S3B A:ICS502 2.2 50.3 1.0
FE3 A:ICS502 2.6 61.5 1.0
FE6 A:ICS502 2.6 57.6 1.0
FE5 A:ICS502 2.6 62.3 1.0
MO1 A:ICS502 2.7 72.5 1.0
FE2 A:ICS502 3.7 57.6 1.0
FE4 A:ICS502 3.7 61.1 1.0
S1B A:ICS502 3.8 59.0 1.0
NH2 A:ARG96 4.0 42.5 1.0
NE A:ARG96 4.2 39.8 1.0
O5 A:HCA501 4.2 48.6 1.0
S2A A:ICS502 4.3 47.9 1.0
S4A A:ICS502 4.3 44.9 1.0
S2B A:ICS502 4.4 47.2 1.0
S3A A:ICS502 4.5 45.1 1.0
CZ A:ARG359 4.6 50.6 1.0
CZ A:ARG96 4.6 35.3 1.0
NE A:ARG359 4.6 51.9 1.0
NH2 A:ARG359 4.6 45.5 1.0
NH1 A:ARG359 5.0 51.3 1.0
FE1 A:ICS502 5.0 67.6 1.0

Iron binding site 8 out of 32 in 9cqy

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Iron binding site 8 out of 32 in the Azotobacter Vinelandii Oxidized Mofep (C2 Symmetry) Obtained Using the Spt Labtech Chameleon


Mono view


Stereo pair view

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

b:67.3
occ:1.00
O D:HOH801 2.0 43.1 1.0
OD2 B:ASP353 2.2 49.5 1.0
OE2 D:GLU109 2.3 50.9 1.0
OD2 B:ASP357 2.4 48.7 1.0
O D:ARG108 2.4 46.1 1.0
O B:HOH918 2.5 49.2 1.0
CG B:ASP353 3.1 48.7 1.0
CG B:ASP357 3.2 45.5 1.0
OD1 B:ASP357 3.2 46.7 1.0
OD1 B:ASP353 3.4 51.9 1.0
CD D:GLU109 3.5 49.3 1.0
C D:ARG108 3.6 40.1 1.0
CG D:GLU109 4.0 44.8 1.0
CB D:ARG108 4.2 37.6 1.0
NZ C:LYS433 4.2 50.9 1.0
CD1 C:PHE429 4.4 42.4 1.0
O B:ASP353 4.4 37.3 1.0
N D:GLU109 4.4 36.4 1.0
CA D:GLU109 4.4 37.6 1.0
CB B:ASP353 4.5 39.6 1.0
OE1 D:GLU109 4.5 48.6 1.0
O B:HOH976 4.5 48.0 1.0
CA D:ARG108 4.5 34.8 1.0
CE C:LYS433 4.6 46.3 1.0
CB B:ASP357 4.6 39.7 1.0
C B:ASP353 4.8 33.3 1.0
O D:PHE107 4.8 41.1 1.0
CB D:GLU109 4.8 43.6 1.0
O D:HOH850 4.8 46.9 1.0
CE1 C:PHE429 4.9 44.3 1.0
O B:HOH787 4.9 54.2 1.0
CG C:PHE429 5.0 43.2 1.0

Iron binding site 9 out of 32 in 9cqy

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Iron binding site 9 out of 32 in the Azotobacter Vinelandii Oxidized Mofep (C2 Symmetry) Obtained Using the Spt Labtech Chameleon


Mono view


Stereo pair view

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

b:47.8
occ:1.00
FE1 B:CLF602 0.0 47.8 1.0
S3A B:CLF602 2.3 27.5 1.0
S2A B:CLF602 2.3 29.6 1.0
SG B:CYS95 2.3 34.5 1.0
S1 B:CLF602 2.5 36.1 1.0
FE2 B:CLF602 2.5 45.5 1.0
FE4 B:CLF602 2.6 54.3 1.0
FE3 B:CLF602 2.7 43.8 1.0
FE8 B:CLF602 3.0 46.0 1.0
N B:CYS95 3.2 28.1 1.0
CB B:CYS95 3.5 19.5 1.0
CA B:CYS95 3.5 23.7 1.0
S4A B:CLF602 3.7 33.3 1.0
C B:GLY94 3.9 25.7 1.0
S4B B:CLF602 4.0 27.9 1.0
O B:HOH872 4.3 36.4 1.0
CA B:GLY94 4.4 25.3 1.0
O B:GLY94 4.6 30.9 1.0
SG A:CYS154 4.6 34.2 1.0
CB B:SER92 4.6 38.6 1.0
SG A:CYS62 4.7 31.6 1.0
N B:GLY94 4.8 27.4 1.0
FE5 B:CLF602 4.9 57.4 1.0
SG A:CYS88 4.9 41.6 1.0

Iron binding site 10 out of 32 in 9cqy

Go back to Iron Binding Sites List in 9cqy
Iron binding site 10 out of 32 in the Azotobacter Vinelandii Oxidized Mofep (C2 Symmetry) Obtained Using the Spt Labtech Chameleon


Mono view


Stereo pair view

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

b:45.5
occ:1.00
FE2 B:CLF602 0.0 45.5 1.0
S2A B:CLF602 2.3 29.6 1.0
S4A B:CLF602 2.3 33.3 1.0
SG A:CYS154 2.3 34.2 1.0
S1 B:CLF602 2.4 36.1 1.0
FE1 B:CLF602 2.5 47.8 1.0
FE4 B:CLF602 2.6 54.3 1.0
FE3 B:CLF602 2.8 43.8 1.0
CB A:CYS154 3.6 34.7 1.0
CA A:GLY185 3.7 36.6 1.0
S3A B:CLF602 3.8 27.5 1.0
O B:HOH872 3.8 36.4 1.0
N A:CYS154 4.1 33.1 1.0
SG B:CYS95 4.1 34.5 1.0
N A:GLY185 4.1 38.2 1.0
FE8 B:CLF602 4.4 46.0 1.0
CA A:CYS154 4.4 36.0 1.0
CB B:SER92 4.5 38.6 1.0
OG B:SER92 4.6 46.9 1.0
C A:GLY185 4.6 38.6 1.0
SG A:CYS62 4.9 31.6 1.0
N A:PHE186 5.0 40.5 1.0

Reference:

B.D.Cook, S.M.Narehood, K.L.Mcguire, Y.Li, F.Akif Tezcan, M.A.Herzik Jr.. Preparation of Oxygen-Sensitive Proteins For High-Resolution Cryoem Structure Determination Using Blot-Free Vitrification. Nat Commun V. 16 3528 2025.
ISSN: ESSN 2041-1723
PubMed: 40229244
DOI: 10.1038/S41467-025-58243-1
Page generated: Fri Aug 8 03:15:54 2025

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