Iron in PDB 9g00: Structure of Carbon Monoxide Dehydrogenase/Acetyl-Coa Synthase (Codh/Acs) in Complex with Corrinoid Iron-Sulfur Protein (Cofesp) From Clostridium Autoethanogenum (Composite Structure, Class 3CB)

Enzymatic activity of Structure of Carbon Monoxide Dehydrogenase/Acetyl-Coa Synthase (Codh/Acs) in Complex with Corrinoid Iron-Sulfur Protein (Cofesp) From Clostridium Autoethanogenum (Composite Structure, Class 3CB)

All present enzymatic activity of Structure of Carbon Monoxide Dehydrogenase/Acetyl-Coa Synthase (Codh/Acs) in Complex with Corrinoid Iron-Sulfur Protein (Cofesp) From Clostridium Autoethanogenum (Composite Structure, Class 3CB):
1.2.7.4; 2.3.1.169;

Other elements in 9g00:

The structure of Structure of Carbon Monoxide Dehydrogenase/Acetyl-Coa Synthase (Codh/Acs) in Complex with Corrinoid Iron-Sulfur Protein (Cofesp) From Clostridium Autoethanogenum (Composite Structure, Class 3CB) also contains other interesting chemical elements:

Cobalt (Co) 1 atom
Nickel (Ni) 4 atoms

Iron Binding Sites:

Pages:

>>> Page 1 <<< Page 2, Binding sites: 11 - 20; Page 3, Binding sites: 21 - 28;

Binding sites:

The binding sites of Iron atom in the Structure of Carbon Monoxide Dehydrogenase/Acetyl-Coa Synthase (Codh/Acs) in Complex with Corrinoid Iron-Sulfur Protein (Cofesp) From Clostridium Autoethanogenum (Composite Structure, Class 3CB) (pdb code 9g00). This binding sites where shown within 5.0 Angstroms radius around Iron atom.
In total 28 binding sites of Iron where determined in the Structure of Carbon Monoxide Dehydrogenase/Acetyl-Coa Synthase (Codh/Acs) in Complex with Corrinoid Iron-Sulfur Protein (Cofesp) From Clostridium Autoethanogenum (Composite Structure, Class 3CB), PDB code: 9g00:
Jump to Iron binding site number: 1; 2; 3; 4; 5; 6; 7; 8; 9; 10;

Iron binding site 1 out of 28 in 9g00

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Iron binding site 1 out of 28 in the Structure of Carbon Monoxide Dehydrogenase/Acetyl-Coa Synthase (Codh/Acs) in Complex with Corrinoid Iron-Sulfur Protein (Cofesp) From Clostridium Autoethanogenum (Composite Structure, Class 3CB)


Mono view


Stereo pair view

A full contact list of Iron with other atoms in the Fe binding site number 1 of Structure of Carbon Monoxide Dehydrogenase/Acetyl-Coa Synthase (Codh/Acs) in Complex with Corrinoid Iron-Sulfur Protein (Cofesp) From Clostridium Autoethanogenum (Composite Structure, Class 3CB) within 5.0Å range:
probe atom residue distance (Å) B Occ
D:Fe801

b:104.7
occ:0.72
 FE1 D:SF4801 0.0 104.7 0.7
SG D:CYS485 2.3 113.3 1.0
S2 D:SF4801 2.3 104.1 0.9
S4 D:SF4801 2.3 103.9 0.8
S3 D:SF4801 2.3 103.6 0.7
FE3 D:SF4801 2.7 105.4 0.9
FE4 D:SF4801 2.7 103.0 0.8
FE2 D:SF4801 2.7 103.9 0.8
CB D:CYS485 3.4 112.9 1.0
S1 D:SF4801 3.9 102.9 0.9
CB D:LEU487 3.9 118.9 1.0
N D:LEU487 4.0 116.0 1.0
C D:CYS485 4.4 116.8 1.0
CA D:LEU487 4.4 116.9 1.0
CA D:CYS485 4.5 115.0 1.0
N D:ASN486 4.6 117.4 1.0
N D:CYS488 4.6 112.7 1.0
SG D:CYS488 4.7 106.9 1.0
CG2 D:VAL510 4.7 121.0 1.0
O D:CYS485 4.7 117.6 1.0
C D:LEU487 4.8 115.4 1.0
SG D:CYS507 4.9 115.2 1.0
CB D:CYS497 5.0 109.2 1.0
SG D:CYS497 5.0 109.0 1.0

Iron binding site 2 out of 28 in 9g00

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Iron binding site 2 out of 28 in the Structure of Carbon Monoxide Dehydrogenase/Acetyl-Coa Synthase (Codh/Acs) in Complex with Corrinoid Iron-Sulfur Protein (Cofesp) From Clostridium Autoethanogenum (Composite Structure, Class 3CB)


Mono view


Stereo pair view

A full contact list of Iron with other atoms in the Fe binding site number 2 of Structure of Carbon Monoxide Dehydrogenase/Acetyl-Coa Synthase (Codh/Acs) in Complex with Corrinoid Iron-Sulfur Protein (Cofesp) From Clostridium Autoethanogenum (Composite Structure, Class 3CB) within 5.0Å range:
probe atom residue distance (Å) B Occ
D:Fe801

b:103.9
occ:0.76
 FE2 D:SF4801 0.0 103.9 0.8
S1 D:SF4801 2.3 102.9 0.9
S4 D:SF4801 2.3 103.9 0.8
S3 D:SF4801 2.3 103.6 0.7
SG D:CYS497 2.4 109.0 1.0
FE3 D:SF4801 2.7 105.4 0.9
FE4 D:SF4801 2.7 103.0 0.8
FE1 D:SF4801 2.7 104.7 0.7
CB D:CYS497 3.0 109.2 1.0
S2 D:SF4801 3.9 104.1 0.9
NI D:NI802 4.0 97.9 0.5
NE2 D:HIS495 4.0 110.6 1.0
SG D:CYS485 4.3 113.3 1.0
CB D:CYS485 4.3 112.9 1.0
CA D:CYS497 4.4 110.8 1.0
O D:CYS485 4.6 117.6 1.0
CD2 D:HIS495 4.6 110.3 1.0
N D:LEU506 4.6 119.2 1.0
SG D:CYS488 4.7 106.9 1.0
N D:CYS497 4.8 111.9 1.0
SG D:CYS507 4.8 115.2 1.0
CA D:GLY505 4.9 123.1 1.0
C D:CYS485 5.0 116.8 1.0

Iron binding site 3 out of 28 in 9g00

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Iron binding site 3 out of 28 in the Structure of Carbon Monoxide Dehydrogenase/Acetyl-Coa Synthase (Codh/Acs) in Complex with Corrinoid Iron-Sulfur Protein (Cofesp) From Clostridium Autoethanogenum (Composite Structure, Class 3CB)


Mono view


Stereo pair view

A full contact list of Iron with other atoms in the Fe binding site number 3 of Structure of Carbon Monoxide Dehydrogenase/Acetyl-Coa Synthase (Codh/Acs) in Complex with Corrinoid Iron-Sulfur Protein (Cofesp) From Clostridium Autoethanogenum (Composite Structure, Class 3CB) within 5.0Å range:
probe atom residue distance (Å) B Occ
D:Fe801

b:105.4
occ:0.87
 FE3 D:SF4801 0.0 105.4 0.9
S4 D:SF4801 2.3 103.9 0.8
S1 D:SF4801 2.3 102.9 0.9
S2 D:SF4801 2.3 104.1 0.9
SG D:CYS507 2.3 115.2 1.0
FE2 D:SF4801 2.7 103.9 0.8
FE1 D:SF4801 2.7 104.7 0.7
FE4 D:SF4801 2.7 103.0 0.8
CB D:CYS507 3.7 115.5 1.0
S3 D:SF4801 3.9 103.6 0.7
N29 F:B12502 4.1 180.4 1.0
CG2 D:VAL510 4.2 121.0 1.0
NI D:NI802 4.2 97.9 0.5
N D:CYS507 4.2 116.4 1.0
CB D:VAL510 4.5 120.4 1.0
CA D:CYS507 4.6 116.0 1.0
SG D:CYS488 4.7 106.9 1.0
SG D:CYS485 4.7 113.3 1.0
N D:LEU506 4.7 119.2 1.0
CA D:GLY505 4.7 123.1 1.0
SG D:CYS497 4.8 109.0 1.0
C D:GLY505 5.0 121.5 1.0
C27 F:B12502 5.0 181.5 1.0
SG D:CYS576 5.0 114.3 1.0

Iron binding site 4 out of 28 in 9g00

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Iron binding site 4 out of 28 in the Structure of Carbon Monoxide Dehydrogenase/Acetyl-Coa Synthase (Codh/Acs) in Complex with Corrinoid Iron-Sulfur Protein (Cofesp) From Clostridium Autoethanogenum (Composite Structure, Class 3CB)


Mono view


Stereo pair view

A full contact list of Iron with other atoms in the Fe binding site number 4 of Structure of Carbon Monoxide Dehydrogenase/Acetyl-Coa Synthase (Codh/Acs) in Complex with Corrinoid Iron-Sulfur Protein (Cofesp) From Clostridium Autoethanogenum (Composite Structure, Class 3CB) within 5.0Å range:
probe atom residue distance (Å) B Occ
D:Fe801

b:103.0
occ:0.75
 FE4 D:SF4801 0.0 103.0 0.8
SG D:CYS488 2.2 106.9 1.0
S3 D:SF4801 2.3 103.6 0.7
S2 D:SF4801 2.3 104.1 0.9
S1 D:SF4801 2.3 102.9 0.9
NI D:NI802 2.4 97.9 0.5
FE1 D:SF4801 2.7 104.7 0.7
FE2 D:SF4801 2.7 103.9 0.8
FE3 D:SF4801 2.7 105.4 0.9
CB D:CYS488 3.2 109.7 1.0
N D:CYS488 3.8 112.7 1.0
S4 D:SF4801 3.9 103.9 0.8
CA D:CYS488 4.1 111.4 1.0
SG D:CYS576 4.1 114.3 1.0
SG D:CYS574 4.3 114.2 1.0
SG D:CYS507 4.4 115.2 1.0
C D:LEU487 4.5 115.4 1.0
SG D:CYS497 4.7 109.0 1.0
NE2 D:HIS495 4.8 110.6 1.0
CD2 D:HIS495 4.9 110.3 1.0
CB D:LEU487 4.9 118.9 1.0
N D:LEU487 4.9 116.0 1.0
SG D:CYS485 4.9 113.3 1.0

Iron binding site 5 out of 28 in 9g00

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Iron binding site 5 out of 28 in the Structure of Carbon Monoxide Dehydrogenase/Acetyl-Coa Synthase (Codh/Acs) in Complex with Corrinoid Iron-Sulfur Protein (Cofesp) From Clostridium Autoethanogenum (Composite Structure, Class 3CB)


Mono view


Stereo pair view

A full contact list of Iron with other atoms in the Fe binding site number 5 of Structure of Carbon Monoxide Dehydrogenase/Acetyl-Coa Synthase (Codh/Acs) in Complex with Corrinoid Iron-Sulfur Protein (Cofesp) From Clostridium Autoethanogenum (Composite Structure, Class 3CB) within 5.0Å range:
probe atom residue distance (Å) B Occ
F:Fe501

b:208.0
occ:1.00
 FE1 F:SF4501 0.0 208.0 1.0
S2 F:SF4501 2.3 207.4 1.0
S4 F:SF4501 2.3 205.6 1.0
S3 F:SF4501 2.3 205.7 1.0
SG F:CYS42 2.3 213.6 1.0
FE2 F:SF4501 2.7 206.1 1.0
FE4 F:SF4501 2.7 208.1 1.0
FE3 F:SF4501 2.7 206.1 1.0
CB F:CYS42 3.6 216.4 1.0
S1 F:SF4501 3.9 204.2 1.0
CA F:CYS42 4.3 218.6 1.0
SG F:CYS17 4.5 208.9 1.0
CG F:PRO13 4.5 196.3 1.0
SG F:CYS25 4.6 199.1 1.0
SG F:CYS20 4.6 208.4 1.0
CG2 F:THR12 4.8 190.5 1.0
CD F:PRO13 4.9 196.3 1.0
CB F:HIS44 4.9 230.7 1.0
CB F:CYS20 5.0 209.7 1.0

Iron binding site 6 out of 28 in 9g00

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Iron binding site 6 out of 28 in the Structure of Carbon Monoxide Dehydrogenase/Acetyl-Coa Synthase (Codh/Acs) in Complex with Corrinoid Iron-Sulfur Protein (Cofesp) From Clostridium Autoethanogenum (Composite Structure, Class 3CB)


Mono view


Stereo pair view

A full contact list of Iron with other atoms in the Fe binding site number 6 of Structure of Carbon Monoxide Dehydrogenase/Acetyl-Coa Synthase (Codh/Acs) in Complex with Corrinoid Iron-Sulfur Protein (Cofesp) From Clostridium Autoethanogenum (Composite Structure, Class 3CB) within 5.0Å range:
probe atom residue distance (Å) B Occ
F:Fe501

b:206.1
occ:1.00
 FE2 F:SF4501 0.0 206.1 1.0
SG F:CYS25 2.2 199.1 1.0
S1 F:SF4501 2.3 204.2 1.0
S3 F:SF4501 2.3 205.7 1.0
S4 F:SF4501 2.3 205.6 1.0
FE4 F:SF4501 2.7 208.1 1.0
FE3 F:SF4501 2.7 206.1 1.0
FE1 F:SF4501 2.7 208.0 1.0
CB F:CYS25 3.4 195.4 1.0
CA F:CYS25 3.6 193.3 1.0
S2 F:SF4501 3.9 207.4 1.0
N F:CYS25 3.9 193.9 1.0
N F:ASN16 4.0 204.9 1.0
CG2 F:THR12 4.3 190.5 1.0
CA F:ASN16 4.5 206.4 1.0
N F:CYS17 4.5 207.3 1.0
N F:LYS15 4.6 201.2 1.0
SG F:CYS17 4.6 208.9 1.0
C F:THR24 4.7 196.0 1.0
SG F:CYS20 4.7 208.4 1.0
SG F:CYS42 4.9 213.6 1.0
O F:THR24 4.9 194.6 1.0
C F:CYS25 4.9 191.3 1.0
C F:LYS15 5.0 203.7 1.0

Iron binding site 7 out of 28 in 9g00

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Iron binding site 7 out of 28 in the Structure of Carbon Monoxide Dehydrogenase/Acetyl-Coa Synthase (Codh/Acs) in Complex with Corrinoid Iron-Sulfur Protein (Cofesp) From Clostridium Autoethanogenum (Composite Structure, Class 3CB)


Mono view


Stereo pair view

A full contact list of Iron with other atoms in the Fe binding site number 7 of Structure of Carbon Monoxide Dehydrogenase/Acetyl-Coa Synthase (Codh/Acs) in Complex with Corrinoid Iron-Sulfur Protein (Cofesp) From Clostridium Autoethanogenum (Composite Structure, Class 3CB) within 5.0Å range:
probe atom residue distance (Å) B Occ
F:Fe501

b:206.1
occ:1.00
 FE3 F:SF4501 0.0 206.1 1.0
SG F:CYS20 2.2 208.4 1.0
S2 F:SF4501 2.3 207.4 1.0
S4 F:SF4501 2.3 205.6 1.0
S1 F:SF4501 2.3 204.2 1.0
FE4 F:SF4501 2.7 208.1 1.0
FE2 F:SF4501 2.7 206.1 1.0
FE1 F:SF4501 2.7 208.0 1.0
CB F:CYS20 3.3 209.7 1.0
N F:CYS20 3.5 211.8 1.0
S3 F:SF4501 3.9 205.7 1.0
CA F:CYS20 4.0 211.4 1.0
N F:ASP19 4.1 210.6 1.0
CB F:PHE28 4.3 195.6 1.0
CG F:PHE28 4.4 196.9 1.0
SG F:CYS42 4.5 213.6 1.0
N F:LYS18 4.6 208.7 1.0
C F:ASP19 4.6 212.1 1.0
O F:PHE22 4.6 213.2 1.0
C F:LYS18 4.7 210.1 1.0
CA F:LYS18 4.7 209.4 1.0
CD1 F:PHE28 4.8 197.1 1.0
CD2 F:PHE28 4.8 197.7 1.0
CA F:ASP19 4.8 211.7 1.0
SG F:CYS25 4.9 199.1 1.0
SG F:CYS17 4.9 208.9 1.0
CB F:CYS42 4.9 216.4 1.0
C F:CYS20 4.9 213.2 1.0

Iron binding site 8 out of 28 in 9g00

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Iron binding site 8 out of 28 in the Structure of Carbon Monoxide Dehydrogenase/Acetyl-Coa Synthase (Codh/Acs) in Complex with Corrinoid Iron-Sulfur Protein (Cofesp) From Clostridium Autoethanogenum (Composite Structure, Class 3CB)


Mono view


Stereo pair view

A full contact list of Iron with other atoms in the Fe binding site number 8 of Structure of Carbon Monoxide Dehydrogenase/Acetyl-Coa Synthase (Codh/Acs) in Complex with Corrinoid Iron-Sulfur Protein (Cofesp) From Clostridium Autoethanogenum (Composite Structure, Class 3CB) within 5.0Å range:
probe atom residue distance (Å) B Occ
F:Fe501

b:208.1
occ:1.00
 FE4 F:SF4501 0.0 208.1 1.0
SG F:CYS17 2.2 208.9 1.0
S1 F:SF4501 2.3 204.2 1.0
S2 F:SF4501 2.3 207.4 1.0
S3 F:SF4501 2.3 205.7 1.0
FE3 F:SF4501 2.7 206.1 1.0
FE2 F:SF4501 2.7 206.1 1.0
FE1 F:SF4501 2.7 208.0 1.0
N F:CYS17 3.5 207.3 1.0
N F:ASP19 3.6 210.6 1.0
N F:LYS18 3.6 208.7 1.0
CB F:CYS17 3.6 208.2 1.0
CA F:CYS17 3.9 207.9 1.0
S4 F:SF4501 3.9 205.6 1.0
C F:CYS17 3.9 208.7 1.0
CB F:ASP19 4.1 211.7 1.0
CA F:ASP19 4.3 211.7 1.0
CA F:LYS18 4.5 209.4 1.0
C F:LYS18 4.5 210.1 1.0
N F:CYS20 4.5 211.8 1.0
CG F:ASP19 4.5 212.5 1.0
C F:ASN16 4.6 207.1 1.0
SG F:CYS25 4.6 199.1 1.0
N F:ASN16 4.7 204.9 1.0
O F:CYS17 4.8 209.4 1.0
SG F:CYS20 4.8 208.4 1.0
SG F:CYS42 4.8 213.6 1.0
OD1 F:ASP19 4.8 213.1 1.0
CD2 F:HIS44 4.9 232.2 1.0
CA F:ASN16 4.9 206.4 1.0
C F:ASP19 5.0 212.1 1.0

Iron binding site 9 out of 28 in 9g00

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Iron binding site 9 out of 28 in the Structure of Carbon Monoxide Dehydrogenase/Acetyl-Coa Synthase (Codh/Acs) in Complex with Corrinoid Iron-Sulfur Protein (Cofesp) From Clostridium Autoethanogenum (Composite Structure, Class 3CB)


Mono view


Stereo pair view

A full contact list of Iron with other atoms in the Fe binding site number 9 of Structure of Carbon Monoxide Dehydrogenase/Acetyl-Coa Synthase (Codh/Acs) in Complex with Corrinoid Iron-Sulfur Protein (Cofesp) From Clostridium Autoethanogenum (Composite Structure, Class 3CB) within 5.0Å range:
probe atom residue distance (Å) B Occ
B:Fe701

b:16.4
occ:1.00
 FE1 B:SF4701 0.0 16.4 1.0
S3 B:SF4701 2.3 18.9 1.0
SG B:CYS38 2.3 20.1 1.0
S4 B:SF4701 2.3 16.3 1.0
S2 B:SF4701 2.3 16.4 1.0
FE4 B:SF4701 2.7 18.6 1.0
FE2 B:SF4701 2.7 18.6 1.0
FE3 B:SF4701 2.7 16.4 1.0
CB B:CYS38 3.2 18.8 1.0
S1 B:SF4701 3.9 18.9 1.0
N B:GLY41 4.1 19.2 1.0
CB B:PHE40 4.3 22.5 1.0
NH1 C:ARG56 4.4 35.5 1.0
CA B:CYS38 4.7 19.3 1.0
CA B:GLY41 4.7 18.9 1.0
SG C:CYS38 4.8 20.1 1.0
SG B:CYS46 4.8 22.3 1.0
CD2 B:PHE40 4.8 25.2 1.0
SG C:CYS46 4.9 22.1 1.0
CB B:CYS46 4.9 20.3 1.0
C B:PHE40 5.0 18.8 1.0

Iron binding site 10 out of 28 in 9g00

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Iron binding site 10 out of 28 in the Structure of Carbon Monoxide Dehydrogenase/Acetyl-Coa Synthase (Codh/Acs) in Complex with Corrinoid Iron-Sulfur Protein (Cofesp) From Clostridium Autoethanogenum (Composite Structure, Class 3CB)


Mono view


Stereo pair view

A full contact list of Iron with other atoms in the Fe binding site number 10 of Structure of Carbon Monoxide Dehydrogenase/Acetyl-Coa Synthase (Codh/Acs) in Complex with Corrinoid Iron-Sulfur Protein (Cofesp) From Clostridium Autoethanogenum (Composite Structure, Class 3CB) within 5.0Å range:
probe atom residue distance (Å) B Occ
B:Fe701

b:18.6
occ:1.00
 FE2 B:SF4701 0.0 18.6 1.0
S4 B:SF4701 2.3 16.3 1.0
S3 B:SF4701 2.3 18.9 1.0
SG C:CYS46 2.3 22.1 1.0
S1 B:SF4701 2.3 18.9 1.0
FE3 B:SF4701 2.7 16.4 1.0
FE1 B:SF4701 2.7 16.4 1.0
FE4 B:SF4701 2.7 18.6 1.0
CB C:CYS46 3.2 20.2 1.0
NH1 B:ARG48 3.6 46.9 1.0
S2 B:SF4701 3.9 16.4 1.0
NH1 C:ARG48 4.1 47.2 1.0
CA C:CYS46 4.6 19.8 1.0
SG B:CYS46 4.7 22.3 1.0
SG B:CYS38 4.8 20.1 1.0
SG C:CYS38 4.8 20.1 1.0
CZ B:ARG48 4.9 42.6 1.0
CB B:CYS38 4.9 18.8 1.0
CB C:PHE40 5.0 22.4 1.0

Reference:

M.D.Yin, O.N.Lemaire, M.Belhamri, J.G.Rosas-Jimenez, G.Hummer, T.Wagner, B.J.Murphy. Snapshots of Acetyl-Coa Synthesis, the Last Step of CO2 Fixation in the Wood-Ljungdahl Pathway Science 2025.
ISSN: ESSN 1095-9203
DOI: 10.1126/SCIENCE.ADR9672
Page generated: Sun Feb 9 07:25:07 2025

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