Structure of PDB 3iaw Chain A

Receptor sequence
>3iawA (length=203) Species: 11685 (HIV-1 M:B_ARV2/SF2) [Search protein sequence]
PQITLWKRPLVTIRIGGQLKEALLDTGADDTVIEELNLPGCWKPKLIGGI
GGFIKVRQYDQIPVEIAGHKAIGTVLVGPTPVNIIGRNLLTQIGATLNFC
GGGGPQITLWKRPLVTIRIGGQLKEALLDTGADDTVIEELNLPGCWKPKL
IGGIAGFIKVRQYDQIPVEIAGHKAIGTVLVGPTPVNIIGRNLLTQIGAT
LNF
3D structure
PDB3iaw Protein conformational dynamics in the mechanism of HIV-1 protease catalysis.
ChainA
Resolution1.61 Å
3D
structure
Catalytic site residues are labeled in the structure
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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 D29 G48 G49 I50 P81 L127 D129 G131 A132 D133 D134 I151 G152 I154 P185 D25 G27 D29 G48 G49 I50 P81 L127 D129 G131 A132 D133 D134 I151 G152 I154 P185 MOAD: Kd=1.57uM
PDBbind-CN: -logKd/Ki=5.80,Kd=1.57uM
Gene Ontology
Molecular Function
GO:0004190 aspartic-type endopeptidase activity
Biological Process
GO:0006508 proteolysis

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Molecular Function
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Biological Process
External links
PDB RCSB:3iaw, PDBe:3iaw, PDBj:3iaw
PDBsum3iaw
PubMed22158985
UniProtP03369|POL_HV1A2 Gag-Pol polyprotein (Gene Name=gag-pol)

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