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Atomistry » Copper » PDB 2aps-2cg1 » 2bw4 » |
Copper in PDB 2bw4: Atomic Resolution Structure of Resting State of the Achromobacter Cycloclastes Cu Nitrite ReductaseEnzymatic activity of Atomic Resolution Structure of Resting State of the Achromobacter Cycloclastes Cu Nitrite Reductase
All present enzymatic activity of Atomic Resolution Structure of Resting State of the Achromobacter Cycloclastes Cu Nitrite Reductase:
1.7.2.1; Protein crystallography data
The structure of Atomic Resolution Structure of Resting State of the Achromobacter Cycloclastes Cu Nitrite Reductase, PDB code: 2bw4
was solved by
S.V.Antonyuk,
R.W.Strange,
G.Sawers,
R.R.Eady,
S.S.Hasnain,
with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:
Copper Binding Sites:
The binding sites of Copper atom in the Atomic Resolution Structure of Resting State of the Achromobacter Cycloclastes Cu Nitrite Reductase
(pdb code 2bw4). This binding sites where shown within
5.0 Angstroms radius around Copper atom.
In total 2 binding sites of Copper where determined in the Atomic Resolution Structure of Resting State of the Achromobacter Cycloclastes Cu Nitrite Reductase, PDB code: 2bw4: Jump to Copper binding site number: 1; 2; Copper binding site 1 out of 2 in 2bw4Go back to![]() ![]()
Copper binding site 1 out
of 2 in the Atomic Resolution Structure of Resting State of the Achromobacter Cycloclastes Cu Nitrite Reductase
![]() Mono view ![]() Stereo pair view
Copper binding site 2 out of 2 in 2bw4Go back to![]() ![]()
Copper binding site 2 out
of 2 in the Atomic Resolution Structure of Resting State of the Achromobacter Cycloclastes Cu Nitrite Reductase
![]() Mono view ![]() Stereo pair view
Reference:
S.V.Antonyuk,
R.W.Strange,
G.Sawers,
R.R.Eady,
S.S.Hasnain.
Atomic Resolution Structures of Resting-State, Substrate- and Product-Complexed Cu-Nitrite Reductase Provide Insight Into Catalytic Mechanism Proc.Natl.Acad.Sci.Usa V. 102 12041 2005.
Page generated: Mon Jul 14 00:48:58 2025
ISSN: ISSN 0027-8424 PubMed: 16093314 DOI: 10.1073/PNAS.0504207102 |
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