Structure of PDB 4dqe Chain A

Receptor sequence
>4dqeA (length=99) Species: 11676 (Human immunodeficiency virus 1) [Search protein sequence]
PQITLWKRPLVTIRICGQLKEALLDTGADDTVIEEMNCPGKWKPKMIGGI
GGFIKVRQYDQIIIEIAGHKAIGTVLVGPTPVNIIGRNLLTQIGATLNF
3D structure
PDB4dqe Hydrophobic core flexibility modulates enzyme activity in HIV-1 protease.
ChainA
Resolution1.3 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 017 A D25 G27 A28 D30 P81 V82 D25 G27 A28 D30 P81 V82
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:4dqe, PDBe:4dqe, PDBj:4dqe
PDBsum4dqe
PubMed22295904
UniProtP12499|POL_HV1Z2 Gag-Pol polyprotein (Gene Name=gag-pol)

[Back to BioLiP]