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Atomistry » Copper » PDB 1mg2-1oe1 » 1oal » |
Copper in PDB 1oal: Active Site Copper and Zinc Ions Modulate the Quaternary Structure of Prokaryotic Cu,Zn Superoxide DismutaseEnzymatic activity of Active Site Copper and Zinc Ions Modulate the Quaternary Structure of Prokaryotic Cu,Zn Superoxide Dismutase
All present enzymatic activity of Active Site Copper and Zinc Ions Modulate the Quaternary Structure of Prokaryotic Cu,Zn Superoxide Dismutase:
1.15.1.1; Protein crystallography data
The structure of Active Site Copper and Zinc Ions Modulate the Quaternary Structure of Prokaryotic Cu,Zn Superoxide Dismutase, PDB code: 1oal
was solved by
P.Cioni,
A.Pesce,
B.M.D.Rocca,
L.Castellifalconiparrilli,
M.Bolognesi,
G.Strambini,
A.Desideri,
with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:
Other elements in 1oal:
The structure of Active Site Copper and Zinc Ions Modulate the Quaternary Structure of Prokaryotic Cu,Zn Superoxide Dismutase also contains other interesting chemical elements:
Copper Binding Sites:
The binding sites of Copper atom in the Active Site Copper and Zinc Ions Modulate the Quaternary Structure of Prokaryotic Cu,Zn Superoxide Dismutase
(pdb code 1oal). This binding sites where shown within
5.0 Angstroms radius around Copper atom.
In total only one binding site of Copper was determined in the Active Site Copper and Zinc Ions Modulate the Quaternary Structure of Prokaryotic Cu,Zn Superoxide Dismutase, PDB code: 1oal: Copper binding site 1 out of 1 in 1oalGo back to![]() ![]()
Copper binding site 1 out
of 1 in the Active Site Copper and Zinc Ions Modulate the Quaternary Structure of Prokaryotic Cu,Zn Superoxide Dismutase
![]() Mono view ![]() Stereo pair view
Reference:
P.Cioni,
A.Pesce,
B.Morozzo Della Rocca,
S.Castelli,
M.Falconi,
L.Parrilli,
M.Bolognesi,
G.Strambini,
A.Desideri.
Active-Site Copper and Zinc Ions Modulate the Quaternary Structure of Prokaryotic Cu,Zn Superoxide Dismutase J.Mol.Biol. V. 326 1351 2003.
Page generated: Mon Jul 14 00:13:01 2025
ISSN: ISSN 0022-2836 PubMed: 12595249 DOI: 10.1016/S0022-2836(03)00047-0 |
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