Structure of PDB 1hvr Chain B

Receptor sequence
>1hvrB (length=99) Species: 11676 (Human immunodeficiency virus 1) [Search protein sequence]
PQVTLWQRPLVTIKIGGQLKEALLDTGADDTVLEEMSLPGRWKPKMIGGI
GGFIKVRQYDQILIEICGHKAIGTVLVGPTPVNIIGRNLLTQIGATLNF
3D structure
PDB1hvr Rational design of potent, bioavailable, nonpeptide cyclic ureas as HIV protease inhibitors.
ChainB
Resolution1.8 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 XK2 B D25 G27 A28 D30 V32 G49 I50 D25 G27 A28 D30 V32 G49 I50 PDBbind-CN: -logKd/Ki=9.51,Ki=0.31nM
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:1hvr, PDBe:1hvr, PDBj:1hvr
PDBsum1hvr
PubMed8278812
UniProtP04585|POL_HV1H2 Gag-Pol polyprotein (Gene Name=gag-pol)

[Back to BioLiP]