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Atomistry » Zinc » PDB 1w56-1wfl » 1wa2 » |
Zinc in PDB 1wa2: Crystal Structure of H313Q Mutant of Alcaligenes Xylosoxidans Nitrite Reductase with Nitrite BoundProtein crystallography data
The structure of Crystal Structure of H313Q Mutant of Alcaligenes Xylosoxidans Nitrite Reductase with Nitrite Bound, PDB code: 1wa2
was solved by
M.L.Barrett,
R.L.Harris,
S.V.Antonyuk,
R.W.Strange,
M.A.Hough,
R.R.Eady,
G.Sawers,
S.S.Hasnain,
with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:
Other elements in 1wa2:
The structure of Crystal Structure of H313Q Mutant of Alcaligenes Xylosoxidans Nitrite Reductase with Nitrite Bound also contains other interesting chemical elements:
Zinc Binding Sites:
The binding sites of Zinc atom in the Crystal Structure of H313Q Mutant of Alcaligenes Xylosoxidans Nitrite Reductase with Nitrite Bound
(pdb code 1wa2). 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 H313Q Mutant of Alcaligenes Xylosoxidans Nitrite Reductase with Nitrite Bound, PDB code: 1wa2: Jump to Zinc binding site number: 1; 2; Zinc binding site 1 out of 2 in 1wa2Go back to Zinc Binding Sites List in 1wa2
Zinc binding site 1 out
of 2 in the Crystal Structure of H313Q Mutant of Alcaligenes Xylosoxidans Nitrite Reductase with Nitrite Bound
Mono view Stereo pair view
Zinc binding site 2 out of 2 in 1wa2Go back to Zinc Binding Sites List in 1wa2
Zinc binding site 2 out
of 2 in the Crystal Structure of H313Q Mutant of Alcaligenes Xylosoxidans Nitrite Reductase with Nitrite Bound
Mono view Stereo pair view
Reference:
M.L.Barrett,
R.L.Harris,
S.V.Antonyuk,
M.A.Hough,
M.J.Ellis,
G.Sawers,
R.R.Eady,
S.S.Hasnain.
Insights Into Redox Partner Interactions and Substrate Binding in Nitrite Reductase From Alcaligenes Xylosoxidans: Crystal Structures of the TRP138HIS and HIS313GLN Mutants Biochemistry V. 43 16311 2004.
Page generated: Wed Dec 16 03:08:42 2020
ISSN: ISSN 0006-2960 PubMed: 15610025 DOI: 10.1021/BI048682G |
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