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Iron in PDB 7mci: Mofe Protein From Azotobacter Vinelandii with A Sulfur-Replenished Cofactor

Enzymatic activity of Mofe Protein From Azotobacter Vinelandii with A Sulfur-Replenished Cofactor

All present enzymatic activity of Mofe Protein From Azotobacter Vinelandii with A Sulfur-Replenished Cofactor:
1.18.6.1;

Protein crystallography data

The structure of Mofe Protein From Azotobacter Vinelandii with A Sulfur-Replenished Cofactor, PDB code: 7mci was solved by W.Kang, C.Lee, Y.Hu, M.W.Ribbe, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 38.22 / 1.65
Space group C 1 2 1
Cell size a, b, c (Å), α, β, γ (°) 166.834, 73.995, 208.766, 90, 103.05, 90
R / Rfree (%) 17.2 / 19.5

Other elements in 7mci:

The structure of Mofe Protein From Azotobacter Vinelandii with A Sulfur-Replenished Cofactor also contains other interesting chemical elements:

Molybdenum (Mo) 8 atoms
Calcium (Ca) 2 atoms

Iron Binding Sites:

Pages:

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

Binding sites:

The binding sites of Iron atom in the Mofe Protein From Azotobacter Vinelandii with A Sulfur-Replenished Cofactor (pdb code 7mci). This binding sites where shown within 5.0 Angstroms radius around Iron atom.
In total 30 binding sites of Iron where determined in the Mofe Protein From Azotobacter Vinelandii with A Sulfur-Replenished Cofactor, PDB code: 7mci:
Jump to Iron binding site number: 1; 2; 3; 4; 5; 6; 7; 8; 9; 10;

Iron binding site 1 out of 30 in 7mci

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Iron binding site 1 out of 30 in the Mofe Protein From Azotobacter Vinelandii with A Sulfur-Replenished Cofactor


Mono view


Stereo pair view

A full contact list of Iron with other atoms in the Fe binding site number 1 of Mofe Protein From Azotobacter Vinelandii with A Sulfur-Replenished Cofactor within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Fe502

b:22.3
occ:1.00
FE1 A:ICS502 0.0 22.3 1.0
S2A A:ICS502 2.2 20.4 1.0
S4A A:ICS502 2.3 21.6 1.0
S1A A:ICS502 2.3 20.2 1.0
SG A:CYS275 2.4 24.5 1.0
FE3 A:ICS502 2.6 21.8 1.0
FE2 A:ICS502 2.6 21.6 1.0
FE4 A:ICS502 2.7 21.3 1.0
CB A:CYS275 3.4 22.3 1.0
CX A:ICS502 3.5 19.4 1.0
OG A:SER278 4.0 22.8 1.0
CB A:LEU358 4.2 21.5 1.0
CB A:SER278 4.4 22.8 1.0
CE2 A:TYR229 4.6 21.6 1.0
CA A:CYS275 4.6 23.5 1.0
CD2 A:LEU358 4.7 23.9 1.0
S2B A:ICS502 4.8 20.4 1.0
S5A A:ICS502 4.8 21.8 1.0
S3A A:ICS502 4.8 20.6 1.0
N A:SER278 4.9 21.7 1.0
FE6 A:ICS502 4.9 20.6 1.0
CD2 A:TYR229 5.0 20.3 1.0

Iron binding site 2 out of 30 in 7mci

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Iron binding site 2 out of 30 in the Mofe Protein From Azotobacter Vinelandii with A Sulfur-Replenished Cofactor


Mono view


Stereo pair view

A full contact list of Iron with other atoms in the Fe binding site number 2 of Mofe Protein From Azotobacter Vinelandii with A Sulfur-Replenished Cofactor within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Fe502

b:21.6
occ:1.00
FE2 A:ICS502 0.0 21.6 1.0
CX A:ICS502 2.0 19.4 1.0
S2B A:ICS502 2.2 20.4 1.0
S2A A:ICS502 2.2 20.4 1.0
S1A A:ICS502 2.3 20.2 1.0
FE6 A:ICS502 2.6 20.6 1.0
FE4 A:ICS502 2.6 21.3 1.0
FE1 A:ICS502 2.6 22.3 1.0
FE3 A:ICS502 2.7 21.8 1.0
FE5 A:ICS502 3.7 20.4 1.0
FE7 A:ICS502 3.7 20.3 1.0
S4A A:ICS502 3.8 21.6 1.0
CZ A:PHE381 4.0 20.4 1.0
NE2 A:HIS195 4.1 23.3 1.0
S3B A:ICS502 4.2 19.7 1.0
CE1 A:HIS195 4.2 23.6 1.0
S1B A:ICS502 4.2 19.2 1.0
CG1 A:VAL70 4.5 23.6 1.0
S3A A:ICS502 4.5 20.6 1.0
CE1 A:PHE381 4.5 22.8 1.0
S5A A:ICS502 4.5 21.8 1.0
SG A:CYS275 4.8 24.5 1.0
CG2 A:VAL70 4.9 23.1 1.0

Iron binding site 3 out of 30 in 7mci

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Iron binding site 3 out of 30 in the Mofe Protein From Azotobacter Vinelandii with A Sulfur-Replenished Cofactor


Mono view


Stereo pair view

A full contact list of Iron with other atoms in the Fe binding site number 3 of Mofe Protein From Azotobacter Vinelandii with A Sulfur-Replenished Cofactor within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Fe502

b:21.8
occ:1.00
FE3 A:ICS502 0.0 21.8 1.0
CX A:ICS502 2.0 19.4 1.0
S5A A:ICS502 2.2 21.8 1.0
S4A A:ICS502 2.2 21.6 1.0
S2A A:ICS502 2.3 20.4 1.0
FE1 A:ICS502 2.6 22.3 1.0
FE7 A:ICS502 2.6 20.3 1.0
FE4 A:ICS502 2.7 21.3 1.0
FE2 A:ICS502 2.7 21.6 1.0
FE6 A:ICS502 3.7 20.6 1.0
FE5 A:ICS502 3.7 20.4 1.0
S1A A:ICS502 3.9 20.2 1.0
NH2 A:ARG96 4.0 21.8 1.0
O A:HOH793 4.1 22.0 1.0
CD2 A:TYR229 4.2 20.3 1.0
S4B A:ICS502 4.2 19.8 1.0
S3B A:ICS502 4.2 19.7 1.0
S2B A:ICS502 4.4 20.4 1.0
CE2 A:TYR229 4.5 21.6 1.0
S3A A:ICS502 4.5 20.6 1.0
SG A:CYS275 4.9 24.5 1.0

Iron binding site 4 out of 30 in 7mci

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Iron binding site 4 out of 30 in the Mofe Protein From Azotobacter Vinelandii with A Sulfur-Replenished Cofactor


Mono view


Stereo pair view

A full contact list of Iron with other atoms in the Fe binding site number 4 of Mofe Protein From Azotobacter Vinelandii with A Sulfur-Replenished Cofactor within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Fe502

b:21.3
occ:1.00
FE4 A:ICS502 0.0 21.3 1.0
CX A:ICS502 2.0 19.4 1.0
S3A A:ICS502 2.2 20.6 1.0
S1A A:ICS502 2.3 20.2 1.0
S4A A:ICS502 2.3 21.6 1.0
FE5 A:ICS502 2.6 20.4 1.0
FE2 A:ICS502 2.6 21.6 1.0
FE3 A:ICS502 2.7 21.8 1.0
FE1 A:ICS502 2.7 22.3 1.0
FE6 A:ICS502 3.7 20.6 1.0
FE7 A:ICS502 3.7 20.3 1.0
S2A A:ICS502 3.8 20.4 1.0
N A:LEU358 4.0 22.2 1.0
N A:GLY357 4.0 22.7 1.0
CB A:LEU358 4.1 21.5 1.0
S4B A:ICS502 4.2 19.8 1.0
S1B A:ICS502 4.3 19.2 1.0
S5A A:ICS502 4.4 21.8 1.0
S2B A:ICS502 4.5 20.4 1.0
CA A:LEU358 4.6 21.3 1.0
N A:ARG359 4.6 22.1 1.0
C A:GLY357 4.6 23.9 1.0
CA A:GLY357 4.7 23.1 1.0
SG A:CYS275 4.8 24.5 1.0
CG A:ARG359 4.8 20.6 1.0
CA A:GLY356 4.9 21.9 1.0
CZ A:PHE381 4.9 20.4 1.0
CD A:ARG359 4.9 20.6 1.0
C A:GLY356 4.9 21.3 1.0

Iron binding site 5 out of 30 in 7mci

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Iron binding site 5 out of 30 in the Mofe Protein From Azotobacter Vinelandii with A Sulfur-Replenished Cofactor


Mono view


Stereo pair view

A full contact list of Iron with other atoms in the Fe binding site number 5 of Mofe Protein From Azotobacter Vinelandii with A Sulfur-Replenished Cofactor within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Fe502

b:20.4
occ:1.00
FE5 A:ICS502 0.0 20.4 1.0
CX A:ICS502 2.0 19.4 1.0
S1B A:ICS502 2.2 19.2 1.0
S4B A:ICS502 2.2 19.8 1.0
S3A A:ICS502 2.3 20.6 1.0
FE6 A:ICS502 2.6 20.6 1.0
FE4 A:ICS502 2.6 21.3 1.0
FE7 A:ICS502 2.6 20.3 1.0
MO1 A:ICS502 2.7 21.8 1.0
FE2 A:ICS502 3.7 21.6 1.0
FE3 A:ICS502 3.7 21.8 1.0
ND1 A:HIS442 3.8 24.2 1.0
S3B A:ICS502 3.8 19.7 1.0
N A:GLY356 4.1 24.0 1.0
CG2 A:ILE355 4.1 23.4 1.0
CA A:GLY356 4.2 21.9 1.0
CE1 A:HIS442 4.2 25.1 1.0
S1A A:ICS502 4.3 20.2 1.0
S4A A:ICS502 4.3 21.6 1.0
S2B A:ICS502 4.4 20.4 1.0
S5A A:ICS502 4.4 21.8 1.0
O7 A:HCA501 4.7 20.3 1.0
N A:GLY357 4.7 22.7 1.0
O5 A:HCA501 4.7 19.8 1.0
CG A:HIS442 4.7 23.0 1.0
CD A:ARG359 4.8 20.6 1.0
CZ A:PHE381 4.9 20.4 1.0
C A:GLY356 5.0 21.3 1.0

Iron binding site 6 out of 30 in 7mci

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Iron binding site 6 out of 30 in the Mofe Protein From Azotobacter Vinelandii with A Sulfur-Replenished Cofactor


Mono view


Stereo pair view

A full contact list of Iron with other atoms in the Fe binding site number 6 of Mofe Protein From Azotobacter Vinelandii with A Sulfur-Replenished Cofactor within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Fe502

b:20.6
occ:1.00
FE6 A:ICS502 0.0 20.6 1.0
CX A:ICS502 2.0 19.4 1.0
S2B A:ICS502 2.2 20.4 1.0
S3B A:ICS502 2.2 19.7 1.0
S1B A:ICS502 2.2 19.2 1.0
FE2 A:ICS502 2.6 21.6 1.0
FE7 A:ICS502 2.6 20.3 1.0
FE5 A:ICS502 2.6 20.4 1.0
MO1 A:ICS502 2.7 21.8 1.0
FE4 A:ICS502 3.7 21.3 1.0
FE3 A:ICS502 3.7 21.8 1.0
S4B A:ICS502 3.8 19.8 1.0
O7 A:HCA501 3.9 20.3 1.0
CZ A:PHE381 4.1 20.4 1.0
S2A A:ICS502 4.2 20.4 1.0
S1A A:ICS502 4.3 20.2 1.0
CG2 A:VAL70 4.4 23.1 1.0
O1 A:HCA501 4.4 20.5 1.0
S5A A:ICS502 4.4 21.8 1.0
O5 A:HCA501 4.5 19.8 1.0
S3A A:ICS502 4.5 20.6 1.0
CE2 A:PHE381 4.6 22.2 1.0
ND1 A:HIS442 4.8 24.2 1.0
C3 A:HCA501 4.8 19.4 1.0
FE1 A:ICS502 4.9 22.3 1.0
C2 A:HCA501 5.0 19.2 1.0

Iron binding site 7 out of 30 in 7mci

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Iron binding site 7 out of 30 in the Mofe Protein From Azotobacter Vinelandii with A Sulfur-Replenished Cofactor


Mono view


Stereo pair view

A full contact list of Iron with other atoms in the Fe binding site number 7 of Mofe Protein From Azotobacter Vinelandii with A Sulfur-Replenished Cofactor within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Fe502

b:20.3
occ:1.00
FE7 A:ICS502 0.0 20.3 1.0
CX A:ICS502 2.0 19.4 1.0
S4B A:ICS502 2.2 19.8 1.0
S5A A:ICS502 2.2 21.8 1.0
S3B A:ICS502 2.2 19.7 1.0
FE6 A:ICS502 2.6 20.6 1.0
FE3 A:ICS502 2.6 21.8 1.0
FE5 A:ICS502 2.6 20.4 1.0
MO1 A:ICS502 2.7 21.8 1.0
O5 A:HCA501 3.7 19.8 1.0
FE2 A:ICS502 3.7 21.6 1.0
FE4 A:ICS502 3.7 21.3 1.0
S1B A:ICS502 3.8 19.2 1.0
O A:HOH738 3.8 19.3 1.0
NE A:ARG96 4.1 19.2 1.0
NH2 A:ARG96 4.2 21.8 1.0
S4A A:ICS502 4.3 21.6 1.0
S2A A:ICS502 4.3 20.4 1.0
S2B A:ICS502 4.4 20.4 1.0
S3A A:ICS502 4.5 20.6 1.0
C7 A:HCA501 4.6 20.9 1.0
CZ A:ARG96 4.7 24.0 1.0
ND1 A:HIS442 4.7 24.2 1.0
O7 A:HCA501 4.7 20.3 1.0
CZ A:ARG359 4.8 22.9 1.0
NH1 A:ARG359 4.8 21.7 1.0
NH2 A:ARG359 5.0 23.2 1.0

Iron binding site 8 out of 30 in 7mci

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Iron binding site 8 out of 30 in the Mofe Protein From Azotobacter Vinelandii with A Sulfur-Replenished Cofactor


Mono view


Stereo pair view

A full contact list of Iron with other atoms in the Fe binding site number 8 of Mofe Protein From Azotobacter Vinelandii with A Sulfur-Replenished Cofactor within 5.0Å range:
probe atom residue distance (Å) B Occ
B:Fe601

b:21.4
occ:1.00
FE1 B:CLF601 0.0 21.4 1.0
S3A B:CLF601 2.3 20.6 1.0
S2A B:CLF601 2.3 21.8 1.0
SG A:CYS154 2.4 24.2 1.0
S1 B:CLF601 2.4 21.5 1.0
FE2 B:CLF601 2.5 23.1 1.0
FE4 B:CLF601 2.6 21.9 1.0
FE3 B:CLF601 2.8 21.6 1.0
CB A:CYS154 3.5 22.7 1.0
O B:HOH925 3.7 22.5 1.0
S4A B:CLF601 3.8 19.8 1.0
N A:CYS154 3.8 21.5 1.0
CA A:GLY185 3.9 22.5 1.0
N A:GLY185 4.1 22.5 1.0
CA A:CYS154 4.2 22.8 1.0
SG B:CYS95 4.3 23.5 1.0
FE8 B:CLF601 4.4 22.0 1.0
OG B:SER92 4.5 33.6 1.0
CB B:SER92 4.5 27.7 1.0
FE5 B:CLF601 4.5 22.1 1.0
SG A:CYS88 4.7 21.5 1.0
C A:GLY185 4.7 25.2 1.0
FE6 B:CLF601 4.8 24.3 1.0
SG B:CYS153 4.9 24.1 1.0
SG A:CYS62 5.0 21.9 1.0
C A:GLU153 5.0 23.5 1.0

Iron binding site 9 out of 30 in 7mci

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Iron binding site 9 out of 30 in the Mofe Protein From Azotobacter Vinelandii with A Sulfur-Replenished Cofactor


Mono view


Stereo pair view

A full contact list of Iron with other atoms in the Fe binding site number 9 of Mofe Protein From Azotobacter Vinelandii with A Sulfur-Replenished Cofactor within 5.0Å range:
probe atom residue distance (Å) B Occ
B:Fe601

b:23.1
occ:1.00
FE2 B:CLF601 0.0 23.1 1.0
S4A B:CLF601 2.3 19.8 1.0
S2A B:CLF601 2.3 21.8 1.0
SG B:CYS95 2.4 23.5 1.0
FE1 B:CLF601 2.5 21.4 1.0
S1 B:CLF601 2.5 21.5 1.0
FE4 B:CLF601 2.6 21.9 1.0
FE3 B:CLF601 2.7 21.6 1.0
FE8 B:CLF601 3.0 22.0 1.0
N B:CYS95 3.3 22.8 1.0
CB B:CYS95 3.6 22.1 1.0
CA B:CYS95 3.6 22.4 1.0
FE5 B:CLF601 3.8 22.1 1.0
S3A B:CLF601 3.8 20.6 1.0
S4B B:CLF601 3.9 20.8 1.0
C B:GLY94 4.0 22.8 1.0
O B:HOH925 4.3 22.5 1.0
CA B:GLY94 4.4 21.0 1.0
FE6 B:CLF601 4.6 24.3 1.0
CB B:SER92 4.6 27.7 1.0
SG A:CYS88 4.6 21.5 1.0
SG A:CYS154 4.6 24.2 1.0
O B:GLY94 4.7 21.7 1.0
SG A:CYS62 4.8 21.9 1.0
N B:GLY94 4.8 22.6 1.0

Iron binding site 10 out of 30 in 7mci

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Iron binding site 10 out of 30 in the Mofe Protein From Azotobacter Vinelandii with A Sulfur-Replenished Cofactor


Mono view


Stereo pair view

A full contact list of Iron with other atoms in the Fe binding site number 10 of Mofe Protein From Azotobacter Vinelandii with A Sulfur-Replenished Cofactor within 5.0Å range:
probe atom residue distance (Å) B Occ
B:Fe601

b:21.6
occ:1.00
FE3 B:CLF601 0.0 21.6 1.0
S4A B:CLF601 2.3 19.8 1.0
S2A B:CLF601 2.3 21.8 1.0
S3A B:CLF601 2.3 20.6 1.0
SG A:CYS62 2.4 21.9 1.0
FE4 B:CLF601 2.6 21.9 1.0
FE2 B:CLF601 2.7 23.1 1.0
FE1 B:CLF601 2.8 21.4 1.0
CB A:CYS62 3.4 21.6 1.0
CA A:GLY185 3.9 22.5 1.0
CB A:TYR64 4.0 20.1 1.0
S1 B:CLF601 4.2 21.5 1.0
CA B:GLY94 4.3 21.0 1.0
C B:GLY94 4.5 22.8 1.0
N A:GLY185 4.5 22.5 1.0
CD1 A:TYR64 4.6 22.0 1.0
CG A:TYR64 4.6 21.1 1.0
N B:CYS95 4.6 22.8 1.0
O B:HOH927 4.8 22.7 1.0
SG A:CYS88 4.8 21.5 1.0
CA A:CYS62 4.8 22.1 1.0
SG A:CYS154 4.8 24.2 1.0
N A:TYR64 4.9 22.5 1.0
CE2 B:TYR98 4.9 22.4 1.0

Reference:

C.C.Lee, W.Kang, A.J.Jasniewski, M.T.Stiebritz, K.Tanifuji, M.W.Ribbe, Y.Hu. Evidence of Substrate Binding and Product Release Via Belt-Sulfur Mobilization of the Nitrogenase Cofactor Nat Catal V. 5 443 2022.
ISSN: ESSN 2520-1158
DOI: 10.1038/S41929-022-00782-7
Page generated: Thu Aug 8 08:25:42 2024

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