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Copper in PDB 1mjg: Crystal Structure of Bifunctional Carbon Monoxide Dehydrogenase/Acetyl-Coa Synthase(Codh/Acs) From Moorella Thermoacetica (F. Clostridium Thermoaceticum)

Enzymatic activity of Crystal Structure of Bifunctional Carbon Monoxide Dehydrogenase/Acetyl-Coa Synthase(Codh/Acs) From Moorella Thermoacetica (F. Clostridium Thermoaceticum)

All present enzymatic activity of Crystal Structure of Bifunctional Carbon Monoxide Dehydrogenase/Acetyl-Coa Synthase(Codh/Acs) From Moorella Thermoacetica (F. Clostridium Thermoaceticum):
1.2.99.2;

Protein crystallography data

The structure of Crystal Structure of Bifunctional Carbon Monoxide Dehydrogenase/Acetyl-Coa Synthase(Codh/Acs) From Moorella Thermoacetica (F. Clostridium Thermoaceticum), PDB code: 1mjg was solved by T.I.Doukov, T.M.Iverson, J.Seravalli, S.W.Ragsdale, C.L.Drennan, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 20.00 / 2.20
Space group P 1
Cell size a, b, c (Å), α, β, γ (°) 99.749, 136.973, 141.532, 101.45, 109.05, 103.94
R / Rfree (%) 21.5 / 24.1

Other elements in 1mjg:

The structure of Crystal Structure of Bifunctional Carbon Monoxide Dehydrogenase/Acetyl-Coa Synthase(Codh/Acs) From Moorella Thermoacetica (F. Clostridium Thermoaceticum) also contains other interesting chemical elements:

Nickel (Ni) 8 atoms
Iron (Fe) 56 atoms

Copper Binding Sites:

The binding sites of Copper atom in the Crystal Structure of Bifunctional Carbon Monoxide Dehydrogenase/Acetyl-Coa Synthase(Codh/Acs) From Moorella Thermoacetica (F. Clostridium Thermoaceticum) (pdb code 1mjg). This binding sites where shown within 5.0 Angstroms radius around Copper atom.
In total 4 binding sites of Copper where determined in the Crystal Structure of Bifunctional Carbon Monoxide Dehydrogenase/Acetyl-Coa Synthase(Codh/Acs) From Moorella Thermoacetica (F. Clostridium Thermoaceticum), PDB code: 1mjg:
Jump to Copper binding site number: 1; 2; 3; 4;

Copper binding site 1 out of 4 in 1mjg

Go back to Copper Binding Sites List in 1mjg
Copper binding site 1 out of 4 in the Crystal Structure of Bifunctional Carbon Monoxide Dehydrogenase/Acetyl-Coa Synthase(Codh/Acs) From Moorella Thermoacetica (F. Clostridium Thermoaceticum)


Mono view


Stereo pair view

A full contact list of Copper with other atoms in the Cu binding site number 1 of Crystal Structure of Bifunctional Carbon Monoxide Dehydrogenase/Acetyl-Coa Synthase(Codh/Acs) From Moorella Thermoacetica (F. Clostridium Thermoaceticum) within 5.0Å range:
probe atom residue distance (Å) B Occ
M:Cu901

b:17.9
occ:1.00
 C M:ACT950 1.9 23.3 1.0
SG M:CYS597 2.1 25.2 1.0
SG M:CYS509 2.2 24.9 1.0
SG M:CYS595 2.4 24.2 1.0
O M:ACT950 2.8 27.2 1.0
NI M:NI902 2.8 9.8 1.0
CH3 M:ACT950 3.0 24.6 1.0
CB M:CYS509 3.2 22.9 1.0
FE4 M:SF4900 3.3 23.0 1.0
CB M:CYS597 3.4 19.9 1.0
CB M:CYS595 3.5 20.4 1.0
S3 M:SF4900 3.5 23.3 1.0
N M:CYS597 4.1 19.0 1.0
CD1 M:ILE146 4.2 31.5 1.0
N M:GLY596 4.3 21.2 1.0
CA M:CYS597 4.5 21.8 1.0
CA M:CYS509 4.6 23.5 1.0
CA M:CYS595 4.7 22.8 1.0
CD1 M:LEU527 4.8 26.3 1.0
CG1 M:VAL149 4.9 21.4 1.0
C M:CYS595 4.9 21.8 1.0

Copper binding site 2 out of 4 in 1mjg

Go back to Copper Binding Sites List in 1mjg
Copper binding site 2 out of 4 in the Crystal Structure of Bifunctional Carbon Monoxide Dehydrogenase/Acetyl-Coa Synthase(Codh/Acs) From Moorella Thermoacetica (F. Clostridium Thermoaceticum)


Mono view


Stereo pair view

A full contact list of Copper with other atoms in the Cu binding site number 2 of Crystal Structure of Bifunctional Carbon Monoxide Dehydrogenase/Acetyl-Coa Synthase(Codh/Acs) From Moorella Thermoacetica (F. Clostridium Thermoaceticum) within 5.0Å range:
probe atom residue distance (Å) B Occ
N:Cu901

b:17.6
occ:1.00
 C N:ACT950 1.8 24.1 1.0
SG N:CYS509 2.2 23.0 1.0
SG N:CYS595 2.2 24.8 1.0
SG N:CYS597 2.2 25.1 1.0
O N:ACT950 2.7 28.0 1.0
NI N:NI902 2.8 11.5 1.0
CH3 N:ACT950 2.9 25.7 1.0
CB N:CYS509 3.2 22.6 1.0
FE4 N:SF4900 3.3 24.4 1.0
S3 N:SF4900 3.4 24.5 1.0
CB N:CYS595 3.4 20.2 1.0
CB N:CYS597 3.5 19.6 1.0
N N:CYS597 4.2 21.7 1.0
CD1 N:ILE146 4.3 33.9 1.0
N N:GLY596 4.3 23.1 1.0
CA N:CYS597 4.5 20.7 1.0
CA N:CYS509 4.6 23.9 1.0
CA N:CYS595 4.7 23.4 1.0
CD1 N:LEU527 4.8 26.4 1.0
S2 N:SF4900 4.9 24.2 1.0
C N:CYS595 4.9 23.2 1.0
CG1 N:VAL149 5.0 22.6 1.0

Copper binding site 3 out of 4 in 1mjg

Go back to Copper Binding Sites List in 1mjg
Copper binding site 3 out of 4 in the Crystal Structure of Bifunctional Carbon Monoxide Dehydrogenase/Acetyl-Coa Synthase(Codh/Acs) From Moorella Thermoacetica (F. Clostridium Thermoaceticum)


Mono view


Stereo pair view

A full contact list of Copper with other atoms in the Cu binding site number 3 of Crystal Structure of Bifunctional Carbon Monoxide Dehydrogenase/Acetyl-Coa Synthase(Codh/Acs) From Moorella Thermoacetica (F. Clostridium Thermoaceticum) within 5.0Å range:
probe atom residue distance (Å) B Occ
O:Cu901

b:87.5
occ:1.00
 C O:ACT950 1.8 87.8 1.0
SG O:CYS597 2.1 87.4 1.0
SG O:CYS595 2.2 88.0 1.0
SG O:CYS509 2.2 87.3 1.0
O O:ACT950 2.6 88.3 1.0
NI O:NI902 2.8 87.4 1.0
CH3 O:ACT950 2.8 88.0 1.0
CB O:CYS595 3.3 88.4 1.0
CB O:CYS509 3.3 86.7 1.0
CB O:CYS597 3.4 87.3 1.0
FE4 O:SF4900 3.5 89.0 1.0
S3 O:SF4900 3.7 88.7 1.0
N O:CYS597 4.0 87.7 1.0
N O:GLY596 4.1 88.5 1.0
CA O:CYS597 4.4 87.2 1.0
CA O:CYS595 4.6 89.0 1.0
CG1 O:VAL149 4.6 74.7 1.0
CA O:CYS509 4.6 86.2 1.0
C O:CYS595 4.7 88.8 1.0
CD1 O:ILE146 4.7 69.7 1.0
CD1 O:LEU527 4.9 91.0 1.0
C O:GLY596 4.9 88.3 1.0
CA O:GLY596 5.0 88.5 1.0

Copper binding site 4 out of 4 in 1mjg

Go back to Copper Binding Sites List in 1mjg
Copper binding site 4 out of 4 in the Crystal Structure of Bifunctional Carbon Monoxide Dehydrogenase/Acetyl-Coa Synthase(Codh/Acs) From Moorella Thermoacetica (F. Clostridium Thermoaceticum)


Mono view


Stereo pair view

A full contact list of Copper with other atoms in the Cu binding site number 4 of Crystal Structure of Bifunctional Carbon Monoxide Dehydrogenase/Acetyl-Coa Synthase(Codh/Acs) From Moorella Thermoacetica (F. Clostridium Thermoaceticum) within 5.0Å range:
probe atom residue distance (Å) B Occ
P:Cu901

b:49.6
occ:1.00
 C P:ACT950 1.8 50.7 1.0
SG P:CYS509 2.2 49.5 1.0
SG P:CYS597 2.2 51.1 1.0
SG P:CYS595 2.2 52.1 1.0
O P:ACT950 2.6 51.7 1.0
NI P:NI902 2.8 49.1 1.0
CH3 P:ACT950 2.8 50.4 1.0
CB P:CYS509 3.2 49.5 1.0
CB P:CYS595 3.4 51.7 1.0
CB P:CYS597 3.4 50.1 1.0
FE4 P:SF4900 3.5 48.4 1.0
S3 P:SF4900 3.6 49.6 1.0
N P:CYS597 4.1 50.4 1.0
N P:GLY596 4.2 52.4 1.0
CA P:CYS597 4.5 50.3 1.0
CD1 P:ILE146 4.5 47.2 1.0
CG1 P:VAL149 4.5 45.5 1.0
CA P:CYS509 4.6 50.3 1.0
CA P:CYS595 4.6 53.0 1.0
C P:CYS595 4.8 52.8 1.0
CD1 P:LEU527 4.9 56.8 1.0

Reference:

T.I.Doukov, T.M.Iverson, J.Seravalli, S.W.Ragsdale, C.L.Drennan. A Ni-Fe-Cu Center in A Bifunctional Carbon Monoxide Dehydrogenase/Acetyl-Coa Synthase Science V. 298 567 2002.
ISSN: ISSN 0036-8075
PubMed: 12386327
DOI: 10.1126/SCIENCE.1075843
Page generated: Mon Jul 14 00:06:22 2025

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