Structure of PDB 3nu4 Chain B

Receptor sequence
>3nu4B (length=99) Species: 11676 (Human immunodeficiency virus 1) [Search protein sequence]
PQITLWKRPLVTIKIGGQLKEALLDTGADDTIIEEMSLPGRWKPKMIGGI
GGFIKVRQYDQIIIEIAGHKAIGTVLVGPTPVNIIGRNLLTQIGATLNF
3D structure
PDB3nu4 Amprenavir complexes with HIV-1 protease and its drug-resistant mutants altering hydrophobic clusters.
ChainB
Resolution1.2 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) D125 T126 G127
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 478 B D125 G127 A128 D130 G149 I150 D25 G27 A28 D30 G49 I50 MOAD: Ki=1.5nM
PDBbind-CN: -logKd/Ki=8.82,Ki=1.5nM
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:3nu4, PDBe:3nu4, PDBj:3nu4
PDBsum3nu4
PubMed20695887
UniProtP03366|POL_HV1B1 Gag-Pol polyprotein (Gene Name=gag-pol)

[Back to BioLiP]