Structure of PDB 2r5q Chain B

Receptor sequence
>2r5qB (length=99) Species: 11676 (Human immunodeficiency virus 1) [Search protein sequence]
PQITLWKRPLVSIKVGGQIKEALLDTGADDTVIEEIALPGRWKPKMIGGI
GGFIKVRQYDQIIIEICGKKAIGTVLVGPTPVNIIGRNMLTQLGCTLNF
3D structure
PDB2r5q The Contribution of Naturally Occurring Polymorphisms in Altering the Biochemical and Structural Characteristics of HIV-1 Subtype C Protease
ChainB
Resolution2.3 Å
3D
structure
Catalytic site residues are labeled in the structure
[Spin on]
[Spin off]
[Reset orientation]

[High quality]
[Low quality]

[White background]
[Black background]

[Download]
[Download structure with residue number starting from 1]
Enzymatic activity
Catalytic site (original residue number in PDB) D25 T26 G27
Catalytic site (residue number reindexed from 1) D25 T26 G27
Enzyme Commision number 2.7.7.-
2.7.7.49: RNA-directed DNA polymerase.
2.7.7.7: DNA-directed DNA polymerase.
3.1.-.-
3.1.13.2: exoribonuclease H.
3.1.26.13: retroviral ribonuclease H.
3.4.23.16: HIV-1 retropepsin.
Interaction with ligand
Site
#		 Ligand Ligand
chain		 Binding residues on receptor
(original residue number in PDB)		 Binding residues on receptor
(residue number reindexed from 1)		 Binding affinity
BS01 1UN B D25 G27 D29 D30 G48 G49 P81 I84 D25 G27 D29 D30 G48 G49 P81 I84 MOAD: Ki=2.7nM
PDBbind-CN: -logKd/Ki=8.57,Ki=2.7nM
Gene Ontology
Molecular Function
GO:0004190 aspartic-type endopeptidase activity
Biological Process
GO:0006508 proteolysis

View graph for
Molecular Function
View graph for
Biological Process
External links
PDB RCSB:2r5q, PDBe:2r5q, PDBj:2r5q
PDBsum2r5q
PubMed18092815
UniProtO12158|POL_HV192 Gag-Pol polyprotein (Gene Name=gag-pol)

[Back to BioLiP]