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Atomistry » Copper » PDB 2xv2-2z7w » 2y1a | |||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Atomistry » Copper » PDB 2xv2-2z7w » 2y1a » |
Copper in PDB 2y1a: Crystal Structure of Achromobacter Cycloclastes Cu Nitrite Reductase with Bound NoEnzymatic activity of Crystal Structure of Achromobacter Cycloclastes Cu Nitrite Reductase with Bound No
All present enzymatic activity of Crystal Structure of Achromobacter Cycloclastes Cu Nitrite Reductase with Bound No:
1.7.2.1; Protein crystallography data
The structure of Crystal Structure of Achromobacter Cycloclastes Cu Nitrite Reductase with Bound No, PDB code: 2y1a
was solved by
M.A.Hough,
S.V.Antonyuk,
with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:
Copper Binding Sites:
The binding sites of Copper atom in the Crystal Structure of Achromobacter Cycloclastes Cu Nitrite Reductase with Bound No
(pdb code 2y1a). 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 Achromobacter Cycloclastes Cu Nitrite Reductase with Bound No, PDB code: 2y1a: Jump to Copper binding site number: 1; 2; Copper binding site 1 out of 2 in 2y1aGo back to![]() ![]()
Copper binding site 1 out
of 2 in the Crystal Structure of Achromobacter Cycloclastes Cu Nitrite Reductase with Bound No
![]() Mono view ![]() Stereo pair view
Copper binding site 2 out of 2 in 2y1aGo back to![]() ![]()
Copper binding site 2 out
of 2 in the Crystal Structure of Achromobacter Cycloclastes Cu Nitrite Reductase with Bound No
![]() Mono view ![]() Stereo pair view
Reference:
S.V.Antonyuk,
M.A.Hough.
Monitoring and Validating Active Site Redox States in Protein Crystals. Biochim.Biophys.Acta V.1814 778 2011.
Page generated: Wed Jul 31 00:18:04 2024
ISSN: ISSN 0006-3002 PubMed: 21215826 DOI: 10.1016/J.BBAPAP.2010.12.017 |
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