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Atomistry » Zinc » PDB 1ed8-1evl » 1et5 » |
Zinc in PDB 1et5: Crystal Structure of Nitrite Reductase ASP98ASN Mutant From Alcaligenes Faecalis S-6Enzymatic activity of Crystal Structure of Nitrite Reductase ASP98ASN Mutant From Alcaligenes Faecalis S-6
All present enzymatic activity of Crystal Structure of Nitrite Reductase ASP98ASN Mutant From Alcaligenes Faecalis S-6:
1.7.99.3; Protein crystallography data
The structure of Crystal Structure of Nitrite Reductase ASP98ASN Mutant From Alcaligenes Faecalis S-6, PDB code: 1et5
was solved by
M.J.Boulanger,
M.Kukimoto,
M.Nishiyama,
S.Horinouchi,
M.E.P.Murphy,
with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:
Other elements in 1et5:
The structure of Crystal Structure of Nitrite Reductase ASP98ASN Mutant From Alcaligenes Faecalis S-6 also contains other interesting chemical elements:
Zinc Binding Sites:
The binding sites of Zinc atom in the Crystal Structure of Nitrite Reductase ASP98ASN Mutant From Alcaligenes Faecalis S-6
(pdb code 1et5). 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 Nitrite Reductase ASP98ASN Mutant From Alcaligenes Faecalis S-6, PDB code: 1et5: Jump to Zinc binding site number: 1; 2; Zinc binding site 1 out of 2 in 1et5Go back to Zinc Binding Sites List in 1et5
Zinc binding site 1 out
of 2 in the Crystal Structure of Nitrite Reductase ASP98ASN Mutant From Alcaligenes Faecalis S-6
Mono view Stereo pair view
Zinc binding site 2 out of 2 in 1et5Go back to Zinc Binding Sites List in 1et5
Zinc binding site 2 out
of 2 in the Crystal Structure of Nitrite Reductase ASP98ASN Mutant From Alcaligenes Faecalis S-6
Mono view Stereo pair view
Reference:
M.J.Boulanger,
M.Kukimoto,
M.Nishiyama,
S.Horinouchi,
M.E.Murphy.
Catalytic Roles For Two Water Bridged Residues (Asp-98 and His-255) in the Active Site of Copper-Containing Nitrite Reductase. J.Biol.Chem. V. 275 23957 2000.
Page generated: Sun Oct 13 00:23:02 2024
ISSN: ISSN 0021-9258 PubMed: 10811642 DOI: 10.1074/JBC.M001859200 |
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