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Atomistry » Nickel » PDB 6cac-6f5r » 6ehq | |||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Atomistry » Nickel » PDB 6cac-6f5r » 6ehq » |
Nickel in PDB 6ehq: E. Coli Hydrogenase-2 (As Isolated Form).Enzymatic activity of E. Coli Hydrogenase-2 (As Isolated Form).
All present enzymatic activity of E. Coli Hydrogenase-2 (As Isolated Form).:
1.12.99.6; Protein crystallography data
The structure of E. Coli Hydrogenase-2 (As Isolated Form)., PDB code: 6ehq
was solved by
S.B.Carr,
S.E.Beaton,
R.M.Evans,
F.A.Armstrong,
with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:
Other elements in 6ehq:
The structure of E. Coli Hydrogenase-2 (As Isolated Form). also contains other interesting chemical elements:
Nickel Binding Sites:
The binding sites of Nickel atom in the E. Coli Hydrogenase-2 (As Isolated Form).
(pdb code 6ehq). This binding sites where shown within
5.0 Angstroms radius around Nickel atom.
In total 2 binding sites of Nickel where determined in the E. Coli Hydrogenase-2 (As Isolated Form)., PDB code: 6ehq: Jump to Nickel binding site number: 1; 2; Nickel binding site 1 out of 2 in 6ehqGo back to Nickel Binding Sites List in 6ehq
Nickel binding site 1 out
of 2 in the E. Coli Hydrogenase-2 (As Isolated Form).
Mono view Stereo pair view
Nickel binding site 2 out of 2 in 6ehqGo back to Nickel Binding Sites List in 6ehq
Nickel binding site 2 out
of 2 in the E. Coli Hydrogenase-2 (As Isolated Form).
Mono view Stereo pair view
Reference:
S.E.Beaton,
R.M.Evans,
A.J.Finney,
C.M.Lamont,
F.A.Armstrong,
F.Sargent,
S.B.Carr.
The Structure of Hydrogenase-2 Fromescherichia Coli: Implications For H2-Driven Proton Pumping. Biochem. J. V. 475 1353 2018.
Page generated: Thu Oct 10 08:23:29 2024
ISSN: ESSN 1470-8728 PubMed: 29555844 DOI: 10.1042/BCJ20180053 |
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