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Atomistry » Copper » PDB 1eso-1haw » 1gs8 » |
Copper in PDB 1gs8: Crystal Structure of Mutant D92N Alcaligenes Xylosoxidans Nitrite ReductaseEnzymatic activity of Crystal Structure of Mutant D92N Alcaligenes Xylosoxidans Nitrite Reductase
All present enzymatic activity of Crystal Structure of Mutant D92N Alcaligenes Xylosoxidans Nitrite Reductase:
1.7.2.1; 1.7.99.3; Protein crystallography data
The structure of Crystal Structure of Mutant D92N Alcaligenes Xylosoxidans Nitrite Reductase, PDB code: 1gs8
was solved by
M.J.Ellis,
M.Prudencio,
F.E.Dodd,
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:
Other elements in 1gs8:
The structure of Crystal Structure of Mutant D92N Alcaligenes Xylosoxidans Nitrite Reductase also contains other interesting chemical elements:
Copper Binding Sites:
The binding sites of Copper atom in the Crystal Structure of Mutant D92N Alcaligenes Xylosoxidans Nitrite Reductase
(pdb code 1gs8). 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 Mutant D92N Alcaligenes Xylosoxidans Nitrite Reductase, PDB code: 1gs8: Jump to Copper binding site number: 1; 2; Copper binding site 1 out of 2 in 1gs8Go back to Copper Binding Sites List in 1gs8
Copper binding site 1 out
of 2 in the Crystal Structure of Mutant D92N Alcaligenes Xylosoxidans Nitrite Reductase
Mono view Stereo pair view
Copper binding site 2 out of 2 in 1gs8Go back to Copper Binding Sites List in 1gs8
Copper binding site 2 out
of 2 in the Crystal Structure of Mutant D92N Alcaligenes Xylosoxidans Nitrite Reductase
Mono view Stereo pair view
Reference:
M.J.Ellis,
M.Prudencio,
F.E.Dodd,
R.W.Strange,
G.Sawers,
R.R.Eady,
S.S.Hasnain.
Biochemical and Crystallographic Studies of the MET144ALA, ASP92ASN and HIS254PHE Mutants of the Nitrite Reductase From Alcaligenes Xylosoxidans Provide Insight Into the Enzyme Mechanism. J.Mol.Biol. V. 316 51 2002.
Page generated: Sun Dec 13 10:59:03 2020
ISSN: ISSN 0022-2836 PubMed: 11829502 DOI: 10.1006/JMBI.2001.5304 |
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