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Atomistry » Chlorine » PDB 2gm1-2h9b » 2gvd | |||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Atomistry » Chlorine » PDB 2gm1-2h9b » 2gvd » |
Chlorine in PDB 2gvd: Complex of Gs- with the Catalytic Domains of Mammalian Adenylyl Cyclase: Complex with Tnp-Atp and MnEnzymatic activity of Complex of Gs- with the Catalytic Domains of Mammalian Adenylyl Cyclase: Complex with Tnp-Atp and Mn
All present enzymatic activity of Complex of Gs- with the Catalytic Domains of Mammalian Adenylyl Cyclase: Complex with Tnp-Atp and Mn:
4.6.1.1; Protein crystallography data
The structure of Complex of Gs- with the Catalytic Domains of Mammalian Adenylyl Cyclase: Complex with Tnp-Atp and Mn, PDB code: 2gvd
was solved by
T.-C.Mou,
S.R.Sprang,
with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:
Other elements in 2gvd:
The structure of Complex of Gs- with the Catalytic Domains of Mammalian Adenylyl Cyclase: Complex with Tnp-Atp and Mn also contains other interesting chemical elements:
Chlorine Binding Sites:
The binding sites of Chlorine atom in the Complex of Gs- with the Catalytic Domains of Mammalian Adenylyl Cyclase: Complex with Tnp-Atp and Mn
(pdb code 2gvd). This binding sites where shown within
5.0 Angstroms radius around Chlorine atom.
In total only one binding site of Chlorine was determined in the Complex of Gs- with the Catalytic Domains of Mammalian Adenylyl Cyclase: Complex with Tnp-Atp and Mn, PDB code: 2gvd: Chlorine binding site 1 out of 1 in 2gvdGo back to Chlorine Binding Sites List in 2gvd
Chlorine binding site 1 out
of 1 in the Complex of Gs- with the Catalytic Domains of Mammalian Adenylyl Cyclase: Complex with Tnp-Atp and Mn
Mono view Stereo pair view
Reference:
T.-C.Mou,
A.Gille,
S.Suryanarayana,
M.Richter,
R.Seifert,
S.R.Sprang.
Broad Specificity of Mammalian Adenylyl Cyclase For Interaction with 2',3'-Substituted Purine- and Pyrimidine Nucleotide Inhibitors. Mol.Pharmacol. V. 70 878 2006.
Page generated: Sat Dec 12 09:06:44 2020
ISSN: ISSN 0026-895X PubMed: 16766715 DOI: 10.1124/MOL.106.026427 |
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