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Atomistry » Copper » PDB 1mg2-1oe1 » 1n62 » |
Copper in PDB 1n62: Crystal Structure of the Mo,Cu-Co Dehydrogenase (Codh), N- Butylisocyanide-Bound StateEnzymatic activity of Crystal Structure of the Mo,Cu-Co Dehydrogenase (Codh), N- Butylisocyanide-Bound State
All present enzymatic activity of Crystal Structure of the Mo,Cu-Co Dehydrogenase (Codh), N- Butylisocyanide-Bound State:
1.2.99.2; Protein crystallography data
The structure of Crystal Structure of the Mo,Cu-Co Dehydrogenase (Codh), N- Butylisocyanide-Bound State, PDB code: 1n62
was solved by
H.Dobbek,
L.Gremer,
R.Kiefersauer,
R.Huber,
O.Meyer,
with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:
Other elements in 1n62:
The structure of Crystal Structure of the Mo,Cu-Co Dehydrogenase (Codh), N- Butylisocyanide-Bound State also contains other interesting chemical elements:
Copper Binding Sites:
The binding sites of Copper atom in the Crystal Structure of the Mo,Cu-Co Dehydrogenase (Codh), N- Butylisocyanide-Bound State
(pdb code 1n62). This binding sites where shown within
5.0 Angstroms radius around Copper atom.
In total 2 binding sites of Copper where determined in the Crystal Structure of the Mo,Cu-Co Dehydrogenase (Codh), N- Butylisocyanide-Bound State, PDB code: 1n62: Jump to Copper binding site number: 1; 2; Copper binding site 1 out of 2 in 1n62Go back to Copper Binding Sites List in 1n62
Copper binding site 1 out
of 2 in the Crystal Structure of the Mo,Cu-Co Dehydrogenase (Codh), N- Butylisocyanide-Bound State
Mono view Stereo pair view
Copper binding site 2 out of 2 in 1n62Go back to Copper Binding Sites List in 1n62
Copper binding site 2 out
of 2 in the Crystal Structure of the Mo,Cu-Co Dehydrogenase (Codh), N- Butylisocyanide-Bound State
Mono view Stereo pair view
Reference:
H.Dobbek,
L.Gremer,
R.Kiefersauer,
R.Huber,
O.Meyer.
Catalysis at A Dinuclear [Cusmo(=O)Oh] Cluster in A Co Dehydrogenase Resolved at 1.1-A Resolution Proc.Natl.Acad.Sci.Usa V. 99 15971 2002.
Page generated: Tue Jul 30 22:22:30 2024
ISSN: ISSN 0027-8424 PubMed: 12475995 DOI: 10.1073/PNAS.212640899 |
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