Structure of PDB 3hlo Chain A

Receptor sequence
>3hloA (length=203) Species: 11685 (HIV-1 M:B_ARV2/SF2) [Search protein sequence]
PQITLWKRPLVTIRIGGQLKEALLDTGADDTVIEELNLPGCWKPKLIGGI
GGFIKVRQYDQIPVEIAGHKAIGTVLVGPTPVNIIGRNLLTQIGATLNFC
GGGGPQITLWKRPLVTIRIGGQLKEALLDTGADDTVIEELNLPGCWKPKL
IGGIAGFIKVRQYDQIPVEIAGHKAIGTVLVGPTPVNIIGRNLLTQIGAT
LNF
3D structure
PDB3hlo Protein conformational dynamics in the mechanism of HIV-1 protease catalysis.
ChainA
Resolution1.6 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 2NC A D25 G27 A28 D29 D30 I47 G48 R112 D129 G131 A132 D133 D134 G152 D25 G27 A28 D29 D30 I47 G48 R112 D129 G131 A132 D133 D134 G152 MOAD: Kd=0.61uM
PDBbind-CN: -logKd/Ki=6.21,Kd=0.61uM
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:3hlo, PDBe:3hlo, PDBj:3hlo
PDBsum3hlo
PubMed22158985
UniProtP03369|POL_HV1A2 Gag-Pol polyprotein (Gene Name=gag-pol)

[Back to BioLiP]