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Atomistry » Copper » PDB 5i26-5luf » 5i6o | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Atomistry » Copper » PDB 5i26-5luf » 5i6o » |
Copper in PDB 5i6o: Crystal Structure of Copper Nitrite Reductase at 100K After 20.70 MgyEnzymatic activity of Crystal Structure of Copper Nitrite Reductase at 100K After 20.70 Mgy
All present enzymatic activity of Crystal Structure of Copper Nitrite Reductase at 100K After 20.70 Mgy:
1.7.2.1; Protein crystallography data
The structure of Crystal Structure of Copper Nitrite Reductase at 100K After 20.70 Mgy, PDB code: 5i6o
was solved by
S.Horrell,
M.A.Hough,
R.W.Strange,
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 Copper Nitrite Reductase at 100K After 20.70 Mgy
(pdb code 5i6o). 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 Copper Nitrite Reductase at 100K After 20.70 Mgy, PDB code: 5i6o: Jump to Copper binding site number: 1; 2; Copper binding site 1 out of 2 in 5i6oGo back to Copper Binding Sites List in 5i6o
Copper binding site 1 out
of 2 in the Crystal Structure of Copper Nitrite Reductase at 100K After 20.70 Mgy
Mono view Stereo pair view
Copper binding site 2 out of 2 in 5i6oGo back to Copper Binding Sites List in 5i6o
Copper binding site 2 out
of 2 in the Crystal Structure of Copper Nitrite Reductase at 100K After 20.70 Mgy
Mono view Stereo pair view
Reference:
S.Horrell,
S.V.Antonyuk,
R.R.Eady,
S.S.Hasnain,
M.A.Hough,
R.W.Strange.
Serial Crystallography Captures Enzyme Catalysis in Copper Nitrite Reductase at Atomic Resolution From One Crystal. Iucrj V. 3 271 2016.
Page generated: Wed Jul 31 04:15:58 2024
ISSN: ESSN 2052-2525 PubMed: 27437114 DOI: 10.1107/S205225251600823X |
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