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Atomistry » Zinc » PDB 1gkr-1h4t » 1gs7 » |
Zinc in PDB 1gs7: Crystal Structure of H254F Mutant of Alcaligenes Xylosoxidans Nitrite ReductaseEnzymatic activity of Crystal Structure of H254F Mutant of Alcaligenes Xylosoxidans Nitrite Reductase
All present enzymatic activity of Crystal Structure of H254F Mutant of Alcaligenes Xylosoxidans Nitrite Reductase:
1.7.2.1; 1.7.99.3; Protein crystallography data
The structure of Crystal Structure of H254F Mutant of Alcaligenes Xylosoxidans Nitrite Reductase, PDB code: 1gs7
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 1gs7:
The structure of Crystal Structure of H254F Mutant of Alcaligenes Xylosoxidans Nitrite Reductase also contains other interesting chemical elements:
Zinc Binding Sites:
The binding sites of Zinc atom in the Crystal Structure of H254F Mutant of Alcaligenes Xylosoxidans Nitrite Reductase
(pdb code 1gs7). This binding sites where shown within
5.0 Angstroms radius around Zinc atom.
In total 2 binding sites of Zinc where determined in the Crystal Structure of H254F Mutant of Alcaligenes Xylosoxidans Nitrite Reductase, PDB code: 1gs7: Jump to Zinc binding site number: 1; 2; Zinc binding site 1 out of 2 in 1gs7Go back to Zinc Binding Sites List in 1gs7
Zinc binding site 1 out
of 2 in the Crystal Structure of H254F Mutant of Alcaligenes Xylosoxidans Nitrite Reductase
Mono view Stereo pair view
Zinc binding site 2 out of 2 in 1gs7Go back to Zinc Binding Sites List in 1gs7
Zinc binding site 2 out
of 2 in the Crystal Structure of H254F Mutant of 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 Oct 13 01:40:40 2024
ISSN: ISSN 0022-2836 PubMed: 11829502 DOI: 10.1006/JMBI.2001.5304 |
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