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

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 3B):
1.2.7.4; 2.3.1.169;

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 3B) also contains other interesting chemical elements:

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

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 3B) (pdb code 9fzz). 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 3B), PDB code: 9fzz:
Jump to Iron binding site number: 1; 2; 3; 4; 5; 6; 7; 8; 9; 10;

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 3B)


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 3B) within 5.0Å range: probe atom residue distance (Å) B Occ D:Fe801 b:89.2 occ:0.86 FE1 D:SF4801 0.0 89.2 0.9 S2 D:SF4801 2.3 88.3 0.7 S4 D:SF4801 2.3 88.4 0.8 S3 D:SF4801 2.3 86.7 0.9 SG D:CYS485 2.3 97.3 1.0 FE2 D:SF4801 2.7 87.5 0.9 FE3 D:SF4801 2.7 90.4 0.8 FE4 D:SF4801 2.7 88.8 1.0 CB D:CYS485 3.0 97.0 1.0 S1 D:SF4801 3.9 88.5 0.8 CB D:LEU487 3.9 100.0 1.0 N D:LEU487 4.1 97.8 1.0 C D:CYS485 4.2 98.8 1.0 CA D:CYS485 4.2 97.7 1.0 O D:CYS485 4.3 99.5 1.0 CG2 D:VAL510 4.3 107.7 1.0 CB D:CYS497 4.5 92.4 1.0 CA D:LEU487 4.6 98.5 1.0 N D:ASN486 4.7 98.7 1.0 N D:CYS488 4.8 96.8 1.0 SG D:CYS507 4.9 101.2 1.0 SG D:CYS497 4.9 90.6 1.0 SG D:CYS488 4.9 94.0 1.0 CD2 D:LEU487 5.0 102.2 1.0

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 3B)


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 3B) within 5.0Å range: probe atom residue distance (Å) B Occ D:Fe801 b:87.5 occ:0.88 FE2 D:SF4801 0.0 87.5 0.9 SG D:CYS497 2.3 90.6 1.0 S3 D:SF4801 2.3 86.7 0.9 S1 D:SF4801 2.3 88.5 0.8 S4 D:SF4801 2.3 88.4 0.8 CB D:CYS497 2.6 92.4 1.0 FE3 D:SF4801 2.7 90.4 0.8 FE1 D:SF4801 2.7 89.2 0.9 FE4 D:SF4801 2.7 88.8 1.0 NE2 D:HIS495 3.8 93.3 1.0 S2 D:SF4801 3.9 88.3 0.7 NI D:NI802 3.9 88.0 0.6 CA D:CYS497 4.1 93.5 1.0 O D:CYS485 4.4 99.5 1.0 CB D:CYS485 4.4 97.0 1.0 CD2 D:HIS495 4.5 94.1 1.0 N D:CYS497 4.6 94.0 1.0 SG D:CYS485 4.6 97.3 1.0 SG D:CYS488 4.7 94.0 1.0 N D:LEU506 4.7 107.2 1.0 SG D:CYS507 4.8 101.2 1.0 CA D:GLY505 4.8 110.2 1.0 CE1 D:HIS495 4.9 93.5 1.0 CG D:LEU506 4.9 107.2 1.0 C D:CYS485 5.0 98.8 1.0

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 3B)


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 3B) within 5.0Å range: probe atom residue distance (Å) B Occ D:Fe801 b:90.4 occ:0.83 FE3 D:SF4801 0.0 90.4 0.8 SG D:CYS507 2.3 101.2 1.0 S4 D:SF4801 2.3 88.4 0.8 S2 D:SF4801 2.3 88.3 0.7 S1 D:SF4801 2.3 88.5 0.8 FE2 D:SF4801 2.7 87.5 0.9 FE1 D:SF4801 2.7 89.2 0.9 FE4 D:SF4801 2.7 88.8 1.0 CB D:CYS507 3.2 104.2 1.0 CG2 D:VAL510 3.7 107.7 1.0 S3 D:SF4801 3.9 86.7 0.9 N D:CYS507 4.0 105.8 1.0 NI D:NI802 4.0 88.0 0.6 CA D:CYS507 4.2 105.7 1.0 CB D:VAL510 4.3 106.7 1.0 SG D:CYS497 4.6 90.6 1.0 SG D:CYS488 4.7 94.0 1.0 CA D:GLY505 4.7 110.2 1.0 C D:GLY505 4.7 108.8 1.0 N D:LEU506 4.8 107.2 1.0 SG D:CYS485 4.9 97.3 1.0

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 3B)


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 3B) within 5.0Å range: probe atom residue distance (Å) B Occ D:Fe801 b:88.8 occ:0.97 FE4 D:SF4801 0.0 88.8 1.0 S3 D:SF4801 2.3 86.7 0.9 S1 D:SF4801 2.3 88.5 0.8 SG D:CYS488 2.3 94.0 1.0 S2 D:SF4801 2.3 88.3 0.7 NI D:NI802 2.5 88.0 0.6 FE3 D:SF4801 2.7 90.4 0.8 FE2 D:SF4801 2.7 87.5 0.9 FE1 D:SF4801 2.7 89.2 0.9 CB D:CYS488 3.3 94.5 1.0 N D:CYS488 3.7 96.8 1.0 S4 D:SF4801 3.9 88.4 0.8 CA D:CYS488 4.1 95.9 1.0 SG D:CYS576 4.3 104.5 1.0 CB D:LEU487 4.4 100.0 1.0 SG D:CYS574 4.4 97.8 1.0 C D:LEU487 4.4 97.9 1.0 SG D:CYS507 4.6 101.2 1.0 CB D:CYS507 4.6 104.2 1.0 N D:LEU487 4.7 97.8 1.0 SG D:CYS497 4.7 90.6 1.0 CA D:LEU487 4.8 98.5 1.0 NE2 D:HIS495 4.8 93.3 1.0 CD2 D:HIS495 4.8 94.1 1.0 SG D:CYS485 4.8 97.3 1.0

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 3B)


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 3B) within 5.0Å range: probe atom residue distance (Å) B Occ B:Fe701 b:16.2 occ:1.00 FE1 B:SF4701 0.0 16.2 1.0 S3 B:SF4701 2.3 18.8 1.0 SG B:CYS38 2.3 19.9 1.0 S4 B:SF4701 2.3 16.2 1.0 S2 B:SF4701 2.3 16.3 1.0 FE4 B:SF4701 2.7 18.4 1.0 FE2 B:SF4701 2.7 18.4 1.0 FE3 B:SF4701 2.7 16.2 1.0 CB B:CYS38 3.2 18.7 1.0 S1 B:SF4701 3.9 18.7 1.0 N B:GLY41 4.1 19.1 1.0 CB B:PHE40 4.3 22.4 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 19.9 1.0 SG B:CYS46 4.8 22.1 1.0 CD2 B:PHE40 4.8 25.1 1.0 SG C:CYS46 4.9 21.9 1.0 CB B:CYS46 4.9 20.1 1.0 C B:PHE40 5.0 18.7 1.0

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 3B)


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 3B) within 5.0Å range: probe atom residue distance (Å) B Occ B:Fe701 b:18.4 occ:1.00 FE2 B:SF4701 0.0 18.4 1.0 S4 B:SF4701 2.3 16.2 1.0 S3 B:SF4701 2.3 18.8 1.0 SG C:CYS46 2.3 21.9 1.0 S1 B:SF4701 2.3 18.7 1.0 FE3 B:SF4701 2.7 16.2 1.0 FE1 B:SF4701 2.7 16.2 1.0 FE4 B:SF4701 2.7 18.4 1.0 CB C:CYS46 3.2 20.0 1.0 NH1 B:ARG48 3.6 46.7 1.0 S2 B:SF4701 3.9 16.3 1.0 NH1 C:ARG48 4.1 47.0 1.0 CA C:CYS46 4.6 19.6 1.0 SG B:CYS46 4.7 22.1 1.0 SG B:CYS38 4.8 19.9 1.0 SG C:CYS38 4.8 19.9 1.0 CZ B:ARG48 4.9 42.4 1.0 CB B:CYS38 4.9 18.7 1.0 CB C:PHE40 5.0 22.3 1.0

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 3B)


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 3B) within 5.0Å range: probe atom residue distance (Å) B Occ B:Fe701 b:16.2 occ:1.00 FE3 B:SF4701 0.0 16.2 1.0 S1 B:SF4701 2.3 18.7 1.0 SG C:CYS38 2.3 19.9 1.0 S4 B:SF4701 2.3 16.2 1.0 S2 B:SF4701 2.3 16.3 1.0 FE2 B:SF4701 2.7 18.4 1.0 FE4 B:SF4701 2.7 18.4 1.0 FE1 B:SF4701 2.7 16.2 1.0 CB C:CYS38 3.2 18.7 1.0 S3 B:SF4701 3.9 18.8 1.0 N C:GLY41 4.1 19.1 1.0 CB C:PHE40 4.3 22.3 1.0 NH1 B:ARG56 4.4 35.3 1.0 CA C:CYS38 4.7 19.2 1.0 CA C:GLY41 4.7 18.8 1.0 CD2 C:PHE40 4.8 25.0 1.0 SG B:CYS38 4.8 19.9 1.0 SG C:CYS46 4.8 21.9 1.0 CB C:CYS46 4.9 20.0 1.0 SG B:CYS46 4.9 22.1 1.0 C C:PHE40 5.0 18.7 1.0

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 3B)


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 3B) within 5.0Å range: probe atom residue distance (Å) B Occ B:Fe701 b:18.4 occ:1.00 FE4 B:SF4701 0.0 18.4 1.0 S2 B:SF4701 2.3 16.3 1.0 S1 B:SF4701 2.3 18.7 1.0 S3 B:SF4701 2.3 18.8 1.0 SG B:CYS46 2.3 22.1 1.0 FE1 B:SF4701 2.7 16.2 1.0 FE3 B:SF4701 2.7 16.2 1.0 FE2 B:SF4701 2.7 18.4 1.0 CB B:CYS46 3.2 20.1 1.0 NH1 C:ARG48 3.6 47.0 1.0 S4 B:SF4701 3.9 16.2 1.0 NH1 B:ARG48 4.1 46.7 1.0 CA B:CYS46 4.6 19.7 1.0 SG C:CYS46 4.7 21.9 1.0 SG C:CYS38 4.8 19.9 1.0 SG B:CYS38 4.8 19.9 1.0 CZ C:ARG48 4.9 42.6 1.0 CB C:CYS38 4.9 18.7 1.0 CB B:PHE40 5.0 22.4 1.0

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 3B)


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 3B) within 5.0Å range: probe atom residue distance (Å) B Occ B:Fe702 b:15.3 occ:1.00 FE1 B:SF4702 0.0 15.3 1.0 S3 B:SF4702 2.3 16.4 1.0 S4 B:SF4702 2.3 14.7 1.0 S2 B:SF4702 2.3 16.6 1.0 SG B:CYS55 2.3 16.1 1.0 FE3 B:SF4702 2.7 15.7 1.0 FE2 B:SF4702 2.7 15.1 1.0 FE4 B:SF4702 2.8 16.8 1.0 CB B:CYS55 3.1 17.0 1.0 N B:ILE69 3.8 17.3 1.0 S1 B:SF4702 3.9 15.8 1.0 CA B:GLY53 4.2 23.5 1.0 CA B:CYS55 4.3 17.7 1.0 N B:CYS55 4.3 18.0 1.0 N B:GLY53 4.3 21.3 1.0 CA B:GLY68 4.4 17.9 1.0 CB B:ILE69 4.5 17.4 1.0 C B:GLY68 4.6 18.1 1.0 N B:CYS70 4.7 16.7 1.0 CA B:ILE69 4.7 17.5 1.0 CB B:CYS47 4.7 16.7 1.0 SG B:CYS47 4.8 16.1 1.0 SG B:CYS70 4.8 16.1 1.0 SG B:CYS50 4.8 19.1 1.0 CG1 B:ILE69 4.9 18.5 1.0 O B:CYS47 5.0 18.6 1.0

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 3B)


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 3B) within 5.0Å range: probe atom residue distance (Å) B Occ B:Fe702 b:15.1 occ:1.00 FE2 B:SF4702 0.0 15.1 1.0 S4 B:SF4702 2.3 14.7 1.0 S3 B:SF4702 2.3 16.4 1.0 S1 B:SF4702 2.3 15.8 1.0 SG B:CYS70 2.3 16.1 1.0 FE4 B:SF4702 2.7 16.8 1.0 FE1 B:SF4702 2.7 15.3 1.0 FE3 B:SF4702 2.8 15.7 1.0 CB B:CYS70 3.2 17.3 1.0 CD1 B:ILE196 3.6 27.5 1.0 N B:CYS70 3.8 16.7 1.0 S2 B:SF4702 3.9 16.6 1.0 CA B:CYS70 4.1 17.1 1.0 NH2 B:ARG80 4.2 21.7 1.0 CB B:ALA72 4.5 21.4 1.0 N B:ILE69 4.6 17.3 1.0 SG B:CYS50 4.7 19.1 1.0 SG B:CYS55 4.8 16.1 1.0 CG1 B:ILE196 4.8 25.7 1.0 SG B:CYS47 4.9 16.1 1.0 C B:CYS70 4.9 18.8 1.0 C B:GLY68 4.9 18.1 1.0 CA B:GLY68 5.0 17.9 1.0 C B:ILE69 5.0 16.6 1.0

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