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Atomistry » Chlorine » PDB 1s8f-1sw5 » 1sdt » |
Chlorine in PDB 1sdt: Crystal Structures of Hiv Protease V82A and L90M Mutants Reveal Changes in Indinavir Binding Site.Enzymatic activity of Crystal Structures of Hiv Protease V82A and L90M Mutants Reveal Changes in Indinavir Binding Site.
All present enzymatic activity of Crystal Structures of Hiv Protease V82A and L90M Mutants Reveal Changes in Indinavir Binding Site.:
3.4.23.16; Protein crystallography data
The structure of Crystal Structures of Hiv Protease V82A and L90M Mutants Reveal Changes in Indinavir Binding Site., PDB code: 1sdt
was solved by
B.Mahalingam,
Y.-F.Wang,
P.I.Boross,
J.Tozser,
J.M.Louis,
R.W.Harrison,
I.T.Weber,
with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:
Chlorine Binding Sites:
The binding sites of Chlorine atom in the Crystal Structures of Hiv Protease V82A and L90M Mutants Reveal Changes in Indinavir Binding Site.
(pdb code 1sdt). This binding sites where shown within
5.0 Angstroms radius around Chlorine atom.
In total 2 binding sites of Chlorine where determined in the Crystal Structures of Hiv Protease V82A and L90M Mutants Reveal Changes in Indinavir Binding Site., PDB code: 1sdt: Jump to Chlorine binding site number: 1; 2; Chlorine binding site 1 out of 2 in 1sdtGo back to Chlorine Binding Sites List in 1sdt
Chlorine binding site 1 out
of 2 in the Crystal Structures of Hiv Protease V82A and L90M Mutants Reveal Changes in Indinavir Binding Site.
Mono view Stereo pair view
Chlorine binding site 2 out of 2 in 1sdtGo back to Chlorine Binding Sites List in 1sdt
Chlorine binding site 2 out
of 2 in the Crystal Structures of Hiv Protease V82A and L90M Mutants Reveal Changes in Indinavir Binding Site.
Mono view Stereo pair view
Reference:
B.Mahalingam,
Y.-F.Wang,
P.I.Boross,
J.Tozser,
J.M.Louis,
R.W.Harrison,
I.T.Weber.
Crystal Structures of Hiv Protease V82A and L90M Mutants Reveal Changes in the Indinavir-Binding Site Eur.J.Biochem. V. 271 1516 2004.
Page generated: Sat Dec 12 08:48:59 2020
ISSN: ISSN 0014-2956 PubMed: 15066177 DOI: 10.1111/J.1432-1033.2004.04060.X |
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