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Atomistry » Calcium » PDB 1zf0-2a2z » 2a2s | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Atomistry » Calcium » PDB 1zf0-2a2z » 2a2s » |
Calcium in PDB 2a2s: Crystal Structure of Human Glutathione Transferase in Complex with S-Nitrosoglutathione in the Absence of Reducing AgentEnzymatic activity of Crystal Structure of Human Glutathione Transferase in Complex with S-Nitrosoglutathione in the Absence of Reducing Agent
All present enzymatic activity of Crystal Structure of Human Glutathione Transferase in Complex with S-Nitrosoglutathione in the Absence of Reducing Agent:
2.5.1.18; Protein crystallography data
The structure of Crystal Structure of Human Glutathione Transferase in Complex with S-Nitrosoglutathione in the Absence of Reducing Agent, PDB code: 2a2s
was solved by
L.J.Parker,
C.J.Morton,
J.J.Adams,
M.W.Parker,
with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:
Calcium Binding Sites:
The binding sites of Calcium atom in the Crystal Structure of Human Glutathione Transferase in Complex with S-Nitrosoglutathione in the Absence of Reducing Agent
(pdb code 2a2s). This binding sites where shown within
5.0 Angstroms radius around Calcium atom.
In total only one binding site of Calcium was determined in the Crystal Structure of Human Glutathione Transferase in Complex with S-Nitrosoglutathione in the Absence of Reducing Agent, PDB code: 2a2s: Calcium binding site 1 out of 1 in 2a2sGo back to![]() ![]()
Calcium binding site 1 out
of 1 in the Crystal Structure of Human Glutathione Transferase in Complex with S-Nitrosoglutathione in the Absence of Reducing Agent
![]() Mono view ![]() Stereo pair view
Reference:
R.Tellez-Sanz,
E.Cesareo,
M.Nuccetelli,
A.M.Aguilera,
C.Baron,
L.J.Parker,
J.J.Adams,
C.J.Morton,
M.Lo Bello,
M.W.Parker,
L.Garcia-Fuentes.
Calorimetric and Structural Studies of the Nitric Oxide Carrier S-Nitrosoglutathione Bound to Human Glutathione Transferase P1-1 Protein Sci. V. 15 1093 2006.
Page generated: Fri Jul 12 08:31:07 2024
ISSN: ISSN 0961-8368 PubMed: 16597834 DOI: 10.1110/PS.052055206 |
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