Iron in PDB 9g7i: Structure of Carbon Monoxide Dehydrogenase/Acetyl-Coa Synthase (Codh/Acs) in Complex with Acetyl-Coenyzme A From Clostridium Autoethanogenum

All present enzymatic activity of Structure of Carbon Monoxide Dehydrogenase/Acetyl-Coa Synthase (Codh/Acs) in Complex with Acetyl-Coenyzme A From Clostridium Autoethanogenum:
1.2.7.4; 2.3.1.169;

The structure of Structure of Carbon Monoxide Dehydrogenase/Acetyl-Coa Synthase (Codh/Acs) in Complex with Acetyl-Coenyzme A From Clostridium Autoethanogenum, PDB code: 9g7i was solved by O.N.Lemaire, M.D.Yin, B.J.Murphy, T.Wagner, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	49.68 / 2.93
Space group	P 42 21 2
Cell size a, b, c (Å), α, β, γ (°)	298.077, 298.077, 127.526, 90, 90, 90
R / Rfree (%)	19 / 22

The structure of Structure of Carbon Monoxide Dehydrogenase/Acetyl-Coa Synthase (Codh/Acs) in Complex with Acetyl-Coenyzme A From Clostridium Autoethanogenum also contains other interesting chemical elements:

Nickel	(Ni)	6 atoms
Chlorine	(Cl)	8 atoms
Calcium	(Ca)	10 atoms

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 Acetyl-Coenyzme A From Clostridium Autoethanogenum (pdb code 9g7i). 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 Acetyl-Coenyzme A From Clostridium Autoethanogenum, PDB code: 9g7i:
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 Acetyl-Coenyzme A From Clostridium Autoethanogenum


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 Acetyl-Coenyzme A From Clostridium Autoethanogenum within 5.0Å range: probe atom residue distance (Å) B Occ A:Fe801 b:149.1 occ:1.00 FE1 A:SF4801 0.0 149.1 1.0 S3 A:SF4801 2.3 99.0 1.0 S2 A:SF4801 2.3 172.6 1.0 S4 A:SF4801 2.3 148.8 1.0 SG A:CYS485 2.5 132.0 1.0 FE4 A:SF4801 2.6 161.8 1.0 FE2 A:SF4801 2.6 169.7 1.0 FE3 A:SF4801 2.6 102.4 1.0 CB A:CYS485 3.3 110.4 1.0 S1 A:SF4801 3.8 181.3 1.0 CG2 A:VAL510 4.4 144.6 1.0 CB A:CYS497 4.6 121.5 1.0 CB A:LEU487 4.6 119.6 1.0 CA A:CYS485 4.6 130.0 1.0 C A:CYS485 4.8 144.3 1.0 CB A:VAL510 4.8 123.0 1.0 SG A:CYS488 4.8 122.2 1.0 N A:LEU487 4.9 143.2 1.0 SG A:CYS507 5.0 138.9 1.0 O A:CYS485 5.0 148.6 1.0

Iron binding site 2 out of 28 in the Structure of Carbon Monoxide Dehydrogenase/Acetyl-Coa Synthase (Codh/Acs) in Complex with Acetyl-Coenyzme A From Clostridium Autoethanogenum


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 Acetyl-Coenyzme A From Clostridium Autoethanogenum within 5.0Å range: probe atom residue distance (Å) B Occ A:Fe801 b:169.7 occ:1.00 FE2 A:SF4801 0.0 169.7 1.0 S1 A:SF4801 2.3 181.3 1.0 S4 A:SF4801 2.3 148.8 1.0 S3 A:SF4801 2.3 99.0 1.0 FE1 A:SF4801 2.6 149.1 1.0 FE4 A:SF4801 2.6 161.8 1.0 FE3 A:SF4801 2.6 102.4 1.0 SG A:CYS497 2.8 132.0 1.0 CB A:CYS497 2.9 121.5 1.0 S2 A:SF4801 3.9 172.6 1.0 N A:LEU506 3.9 127.6 1.0 CA A:GLY505 3.9 122.8 1.0 NE2 A:HIS495 4.2 121.2 1.0 C A:GLY505 4.2 126.4 1.0 CA A:CYS497 4.5 120.3 1.0 N A:CYS507 4.5 125.3 1.0 CB A:CYS485 4.7 110.4 1.0 NI A:NI803 4.7 183.3 1.0 SG A:CYS485 4.7 132.0 1.0 SG A:CYS488 4.8 122.2 1.0 CA A:LEU506 4.9 108.9 1.0 SG A:CYS507 4.9 138.9 1.0 CB A:LEU506 4.9 116.8 1.0 CD2 A:HIS495 5.0 125.5 1.0

Iron binding site 3 out of 28 in the Structure of Carbon Monoxide Dehydrogenase/Acetyl-Coa Synthase (Codh/Acs) in Complex with Acetyl-Coenyzme A From Clostridium Autoethanogenum


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 Acetyl-Coenyzme A From Clostridium Autoethanogenum within 5.0Å range: probe atom residue distance (Å) B Occ A:Fe801 b:102.4 occ:1.00 FE3 A:SF4801 0.0 102.4 1.0 S4 A:SF4801 2.3 148.8 1.0 S1 A:SF4801 2.3 181.3 1.0 S2 A:SF4801 2.3 172.6 1.0 SG A:CYS507 2.5 138.9 1.0 FE1 A:SF4801 2.6 149.1 1.0 FE2 A:SF4801 2.6 169.7 1.0 FE4 A:SF4801 2.6 161.8 1.0 CB A:CYS507 3.3 143.3 1.0 N A:CYS507 3.8 125.3 1.0 S3 A:SF4801 3.9 99.0 1.0 CG2 A:VAL510 4.1 144.6 1.0 CA A:CYS507 4.1 126.2 1.0 CB A:VAL510 4.3 123.0 1.0 CA A:GLY505 4.4 122.8 1.0 C A:GLY505 4.4 126.4 1.0 NH2 A:ARG383 4.6 135.8 1.0 N A:LEU506 4.6 127.6 1.0 NE A:ARG383 4.6 125.5 1.0 NI A:NI803 4.7 183.3 1.0 CZ A:ARG383 4.7 132.0 1.0 O A:GLY505 4.8 125.8 1.0 SG A:CYS488 4.8 122.2 1.0 SG A:CYS576 4.9 110.3 1.0 N A:VAL510 4.9 139.2 1.0 C A:LEU506 4.9 115.4 1.0

Iron binding site 4 out of 28 in the Structure of Carbon Monoxide Dehydrogenase/Acetyl-Coa Synthase (Codh/Acs) in Complex with Acetyl-Coenyzme A From Clostridium Autoethanogenum


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 Acetyl-Coenyzme A From Clostridium Autoethanogenum within 5.0Å range: probe atom residue distance (Å) B Occ A:Fe801 b:161.8 occ:1.00 FE4 A:SF4801 0.0 161.8 1.0 S3 A:SF4801 2.3 99.0 1.0 S2 A:SF4801 2.3 172.6 1.0 S1 A:SF4801 2.3 181.3 1.0 SG A:CYS488 2.4 122.2 1.0 FE1 A:SF4801 2.6 149.1 1.0 FE2 A:SF4801 2.6 169.7 1.0 FE3 A:SF4801 2.6 102.4 1.0 NI A:NI803 3.2 183.3 1.0 CB A:CYS488 3.6 131.4 1.0 S4 A:SF4801 3.9 148.8 1.0 N A:CYS488 4.2 136.0 1.0 SG A:CYS576 4.3 110.3 1.0 CA A:CYS488 4.4 124.2 1.0 SG A:CYS574 4.5 139.6 1.0 CB A:CYS507 4.6 143.3 1.0 NE2 A:HIS495 4.6 121.2 1.0 SG A:CYS485 4.7 132.0 1.0 NH2 A:ARG383 4.7 135.8 1.0 SG A:CYS507 4.7 138.9 1.0 OH A:TYR387 4.9 150.8 1.0 CB A:CYS497 4.9 121.5 1.0 CD2 A:HIS495 4.9 125.5 1.0

Iron binding site 5 out of 28 in the Structure of Carbon Monoxide Dehydrogenase/Acetyl-Coa Synthase (Codh/Acs) in Complex with Acetyl-Coenyzme A From Clostridium Autoethanogenum


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 Acetyl-Coenyzme A From Clostridium Autoethanogenum within 5.0Å range: probe atom residue distance (Å) B Occ B:Fe702 b:55.3 occ:1.00 FE1 B:SF4702 0.0 55.3 1.0 SG B:CYS55 2.2 65.4 1.0 S3 B:SF4702 2.3 74.5 1.0 S2 B:SF4702 2.3 69.1 1.0 S4 B:SF4702 2.3 72.0 1.0 FE4 B:SF4702 2.6 55.6 1.0 FE3 B:SF4702 2.6 62.9 1.0 FE2 B:SF4702 2.7 54.1 1.0 CB B:CYS55 3.5 51.0 1.0 N B:ILE69 3.8 72.9 1.0 S1 B:SF4702 3.9 53.7 1.0 CA B:GLY53 4.2 52.4 1.0 N B:GLY53 4.2 68.8 1.0 CB B:ILE69 4.2 61.0 1.0 SG B:CYS50 4.3 55.6 1.0 CA B:ILE69 4.5 60.1 1.0 N B:CYS70 4.5 61.6 1.0 CG1 B:ILE69 4.6 55.5 1.0 N B:CYS55 4.7 59.1 1.0 C B:GLY68 4.7 70.4 1.0 CA B:CYS55 4.7 59.2 1.0 CA B:GLY68 4.7 64.2 1.0 SG B:CYS70 4.7 53.9 1.0 C B:MET52 4.7 63.7 1.0 O B:CYS47 4.8 72.7 1.0 CB B:MET52 4.9 57.3 1.0

Iron binding site 6 out of 28 in the Structure of Carbon Monoxide Dehydrogenase/Acetyl-Coa Synthase (Codh/Acs) in Complex with Acetyl-Coenyzme A From Clostridium Autoethanogenum


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 Acetyl-Coenyzme A From Clostridium Autoethanogenum within 5.0Å range: probe atom residue distance (Å) B Occ B:Fe702 b:54.1 occ:1.00 FE2 B:SF4702 0.0 54.1 1.0 S4 B:SF4702 2.3 72.0 1.0 S1 B:SF4702 2.3 53.7 1.0 S3 B:SF4702 2.3 74.5 1.0 SG B:CYS70 2.4 53.9 1.0 FE1 B:SF4702 2.7 55.3 1.0 FE3 B:SF4702 2.7 62.9 1.0 FE4 B:SF4702 2.7 55.6 1.0 CB B:CYS70 3.6 55.5 1.0 N B:CYS70 3.9 61.6 1.0 S2 B:SF4702 3.9 69.1 1.0 NH2 B:ARG80 4.0 74.5 1.0 N B:ILE69 4.3 72.9 1.0 CA B:CYS70 4.3 56.8 1.0 CB B:ALA72 4.3 70.7 1.0 SG B:CYS47 4.6 76.0 1.0 SG B:CYS55 4.6 65.4 1.0 CG1 B:ILE196 4.6 62.9 1.0 CA B:GLY68 4.7 64.2 1.0 SG B:CYS50 4.7 55.6 1.0 C B:GLY68 4.8 70.4 1.0 C B:ILE69 5.0 61.0 1.0

Iron binding site 7 out of 28 in the Structure of Carbon Monoxide Dehydrogenase/Acetyl-Coa Synthase (Codh/Acs) in Complex with Acetyl-Coenyzme A From Clostridium Autoethanogenum


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 Acetyl-Coenyzme A From Clostridium Autoethanogenum within 5.0Å range: probe atom residue distance (Å) B Occ B:Fe702 b:62.9 occ:1.00 FE3 B:SF4702 0.0 62.9 1.0 S2 B:SF4702 2.3 69.1 1.0 S1 B:SF4702 2.3 53.7 1.0 S4 B:SF4702 2.3 72.0 1.0 SG B:CYS47 2.4 76.0 1.0 FE4 B:SF4702 2.6 55.6 1.0 FE1 B:SF4702 2.6 55.3 1.0 FE2 B:SF4702 2.7 54.1 1.0 CB B:CYS47 2.9 65.8 1.0 O B:CYS47 3.7 72.7 1.0 C B:CYS47 3.8 70.1 1.0 S3 B:SF4702 3.9 74.5 1.0 CA B:CYS47 3.9 53.7 1.0 NH2 B:ARG80 4.0 74.5 1.0 SG B:CYS55 4.1 65.4 1.0 N B:ASN49 4.2 55.5 1.0 N B:ARG48 4.3 61.0 1.0 CB B:CYS55 4.4 51.0 1.0 CB B:ASN49 4.9 53.9 1.0 SG B:CYS50 4.9 55.6 1.0 CA B:ARG48 4.9 59.2 1.0 N B:CYS47 4.9 54.7 1.0 N B:CYS50 4.9 47.7 1.0 SG B:CYS70 5.0 53.9 1.0 CA B:ASN49 5.0 58.6 1.0

Iron binding site 8 out of 28 in the Structure of Carbon Monoxide Dehydrogenase/Acetyl-Coa Synthase (Codh/Acs) in Complex with Acetyl-Coenyzme A From Clostridium Autoethanogenum


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 Acetyl-Coenyzme A From Clostridium Autoethanogenum within 5.0Å range: probe atom residue distance (Å) B Occ B:Fe702 b:55.6 occ:1.00 FE4 B:SF4702 0.0 55.6 1.0 S2 B:SF4702 2.3 69.1 1.0 S1 B:SF4702 2.3 53.7 1.0 S3 B:SF4702 2.3 74.5 1.0 SG B:CYS50 2.4 55.6 1.0 FE3 B:SF4702 2.6 62.9 1.0 FE1 B:SF4702 2.6 55.3 1.0 FE2 B:SF4702 2.7 54.1 1.0 CB B:CYS50 3.5 64.7 1.0 N B:CYS50 3.8 47.7 1.0 S4 B:SF4702 3.9 72.0 1.0 CG1 B:ILE196 4.0 62.9 1.0 CA B:CYS50 4.1 60.1 1.0 O B:CYS50 4.3 57.8 1.0 C B:ASN49 4.4 58.0 1.0 SG B:CYS70 4.4 53.9 1.0 C B:CYS50 4.5 56.1 1.0 SG B:CYS47 4.6 76.0 1.0 N B:ASN49 4.6 55.5 1.0 N B:GLY53 4.7 68.8 1.0 SG B:CYS55 4.7 65.4 1.0 CB B:ILE196 4.8 64.4 1.0 CB B:MET52 4.8 57.3 1.0 CA B:ASN49 4.9 58.6 1.0 CB B:ASN49 5.0 53.9 1.0

Iron binding site 9 out of 28 in the Structure of Carbon Monoxide Dehydrogenase/Acetyl-Coa Synthase (Codh/Acs) in Complex with Acetyl-Coenyzme A From Clostridium Autoethanogenum


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 Acetyl-Coenyzme A From Clostridium Autoethanogenum within 5.0Å range: probe atom residue distance (Å) B Occ B:Fe705 b:64.9 occ:1.00 FE1 B:XCC705 0.0 64.9 1.0 S2 B:XCC705 2.1 45.8 1.0 S3 B:XCC705 2.1 55.5 1.0 S4 B:XCC705 2.2 53.0 1.0 SG B:CYS333 2.4 56.5 1.0 FE3 B:XCC705 3.2 69.3 1.0 CB B:CYS333 3.3 38.3 1.0 FE4 B:XCC705 3.3 60.6 1.0 FE2 B:XCC705 3.6 75.7 1.0 NE2 B:HIS259 3.6 66.4 1.0 CE1 B:HIS259 3.7 84.7 1.0 S1 B:XCC705 3.7 62.3 1.0 NZ B:LYS560 3.9 60.0 1.0 NI B:XCC705 4.1 88.0 1.0 CE B:LYS560 4.2 54.9 1.0 CA B:CYS333 4.7 48.1 1.0 CB B:CYS451 4.7 54.7 1.0 CB B:SER558 4.7 50.1 1.0 OG B:SER558 4.9 60.7 1.0 ND1 B:HIS259 4.9 57.2 1.0 CD2 B:HIS259 5.0 54.9 1.0 CD1 B:PHE312 5.0 57.4 1.0

Iron binding site 10 out of 28 in the Structure of Carbon Monoxide Dehydrogenase/Acetyl-Coa Synthase (Codh/Acs) in Complex with Acetyl-Coenyzme A From Clostridium Autoethanogenum


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 Acetyl-Coenyzme A From Clostridium Autoethanogenum within 5.0Å range: probe atom residue distance (Å) B Occ B:Fe705 b:75.7 occ:1.00 FE2 B:XCC705 0.0 75.7 1.0 S3 B:XCC705 2.1 55.5 1.0 SG B:CYS295 2.2 85.0 1.0 NE2 B:HIS259 2.4 66.4 1.0 NI B:XCC705 2.6 88.0 1.0 CD2 B:HIS259 3.2 54.9 1.0 CB B:CYS295 3.3 50.3 1.0 CE1 B:HIS259 3.3 84.7 1.0 S4 B:XCC705 3.5 53.0 1.0 S1 B:XCC705 3.5 62.3 1.0 FE4 B:XCC705 3.5 60.6 1.0 FE1 B:XCC705 3.6 64.9 1.0 N B:CYS295 3.9 53.1 1.0 CA B:CYS295 4.1 48.7 1.0 SG B:CYS523 4.3 111.2 1.0 NZ B:LYS560 4.3 60.0 1.0 CG B:HIS259 4.3 46.3 1.0 S2 B:XCC705 4.3 45.8 1.0 ND1 B:HIS259 4.3 57.2 1.0 CB B:CYS523 4.7 49.5 1.0 FE3 B:XCC705 4.7 69.3 1.0 C B:CYS294 5.0 51.8 1.0 CB B:CYS294 5.0 59.1 1.0

M.D.Yin, O.N.Lemaire, J.G.Rosas Jimenez, M.Belhamri, A.Shevchenko, G.Hummer, T.Wagner, B.J.Murphy. Conformational Dynamics of A Multienzyme Complex in Anaerobic Carbon Fixation. Science V. 387 498 2025.
ISSN: ESSN 1095-9203
PubMed: 39883773
DOI: 10.1126/SCIENCE.ADR9672