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Atomistry » Copper » PDB 8po9-8s5x » 8rfx » |
Copper in PDB 8rfx: High pH (8.0) As-Isolated Msox Movie Series Dataset 5 of the Copper Nitrite Reductase From Bradyrhizobium Sp. ORS375 (Two-Domain)[3.40 Mgy]Protein crystallography data
The structure of High pH (8.0) As-Isolated Msox Movie Series Dataset 5 of the Copper Nitrite Reductase From Bradyrhizobium Sp. ORS375 (Two-Domain)[3.40 Mgy], PDB code: 8rfx
was solved by
S.L.Rose,
F.M.Ferroni,
S.V.Antonyuk,
R.R.Eady,
S.S.Hasnain,
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 High pH (8.0) As-Isolated Msox Movie Series Dataset 5 of the Copper Nitrite Reductase From Bradyrhizobium Sp. ORS375 (Two-Domain)[3.40 Mgy]
(pdb code 8rfx). This binding sites where shown within
5.0 Angstroms radius around Copper atom.
In total 2 binding sites of Copper where determined in the High pH (8.0) As-Isolated Msox Movie Series Dataset 5 of the Copper Nitrite Reductase From Bradyrhizobium Sp. ORS375 (Two-Domain)[3.40 Mgy], PDB code: 8rfx: Jump to Copper binding site number: 1; 2; Copper binding site 1 out of 2 in 8rfxGo back to Copper Binding Sites List in 8rfx
Copper binding site 1 out
of 2 in the High pH (8.0) As-Isolated Msox Movie Series Dataset 5 of the Copper Nitrite Reductase From Bradyrhizobium Sp. ORS375 (Two-Domain)[3.40 Mgy]
Mono view Stereo pair view
Copper binding site 2 out of 2 in 8rfxGo back to Copper Binding Sites List in 8rfx
Copper binding site 2 out
of 2 in the High pH (8.0) As-Isolated Msox Movie Series Dataset 5 of the Copper Nitrite Reductase From Bradyrhizobium Sp. ORS375 (Two-Domain)[3.40 Mgy]
Mono view Stereo pair view
Reference:
S.L.Rose,
F.Martin Ferroni,
S.Horrell,
C.Dante Brondino,
R.R.Eady,
S.Jaho,
M.A.Hough,
R.L.Owen,
S.V.Antonyuk,
S.Samar Hasnain.
Spectroscopically Validated pH-Dependent Msox Movies Provide Detailed Mechanism of Copper Nitrite Reductases. J.Mol.Biol. 68706 2024.
Page generated: Wed Jul 31 10:12:01 2024
ISSN: ESSN 1089-8638 PubMed: 39002715 DOI: 10.1016/J.JMB.2024.168706 |
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