Atomistry » Copper » PDB 1mg2-1oe1 » 1mjg
Atomistry »
  Copper »
    PDB 1mg2-1oe1 »
      1mjg »

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: Tue Jul 30 22:22:31 2024

Last articles

Zn in 9JYW
Zn in 9IR4
Zn in 9IR3
Zn in 9GMX
Zn in 9GMW
Zn in 9JEJ
Zn in 9ERF
Zn in 9ERE
Zn in 9EGV
Zn in 9EGW
© Copyright 2008-2020 by atomistry.com
Home   |    Site Map   |    Copyright   |    Contact us   |    Privacy