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Atomistry » Chlorine » PDB 5hq1-5i13 » 5hvp » |
Chlorine in PDB 5hvp: Crystallographic Analysis of A Complex Between Human Immunodeficiency Virus Type 1 Protease and Acetyl-Pepstatin at 2.0-Angstroms ResolutionProtein crystallography data
The structure of Crystallographic Analysis of A Complex Between Human Immunodeficiency Virus Type 1 Protease and Acetyl-Pepstatin at 2.0-Angstroms Resolution, PDB code: 5hvp
was solved by
P.M.D.Fitzgerald,
B.M.Mckeever,
J.F.Vanmiddlesworth,
J.P.Springer,
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 Crystallographic Analysis of A Complex Between Human Immunodeficiency Virus Type 1 Protease and Acetyl-Pepstatin at 2.0-Angstroms Resolution
(pdb code 5hvp). This binding sites where shown within
5.0 Angstroms radius around Chlorine atom.
In total 2 binding sites of Chlorine where determined in the Crystallographic Analysis of A Complex Between Human Immunodeficiency Virus Type 1 Protease and Acetyl-Pepstatin at 2.0-Angstroms Resolution, PDB code: 5hvp: Jump to Chlorine binding site number: 1; 2; Chlorine binding site 1 out of 2 in 5hvpGo back to Chlorine Binding Sites List in 5hvp
Chlorine binding site 1 out
of 2 in the Crystallographic Analysis of A Complex Between Human Immunodeficiency Virus Type 1 Protease and Acetyl-Pepstatin at 2.0-Angstroms Resolution
Mono view Stereo pair view
Chlorine binding site 2 out of 2 in 5hvpGo back to Chlorine Binding Sites List in 5hvp
Chlorine binding site 2 out
of 2 in the Crystallographic Analysis of A Complex Between Human Immunodeficiency Virus Type 1 Protease and Acetyl-Pepstatin at 2.0-Angstroms Resolution
Mono view Stereo pair view
Reference:
P.M.Fitzgerald,
B.M.Mckeever,
J.F.Vanmiddlesworth,
J.P.Springer,
J.C.Heimbach,
C.T.Leu,
W.K.Herber,
R.A.Dixon,
P.L.Darke.
Crystallographic Analysis of A Complex Between Human Immunodeficiency Virus Type 1 Protease and Acetyl-Pepstatin at 2.0-A Resolution. J.Biol.Chem. V. 265 14209 1990.
Page generated: Sat Dec 12 11:49:23 2020
ISSN: ISSN 0021-9258 PubMed: 2201682 |
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