Structure of PDB 2pyn Chain B

Receptor sequence
>2pynB (length=99) Species: 11676 (Human immunodeficiency virus 1) [Search protein sequence]
PQITLWQRPLVTIKIGGQLKEALLDTGADNTVLEEMSLPGAWKPKMIGGI
GGFIKVRQYDQILIEICGHKVIGTVLVGPTPVNIIGRNLLTQIGCTLNF
3D structure
PDB2pyn Molecular analysis of the HIV-1 resistance development: enzymatic activities, crystal structures, and thermodynamics of nelfinavir-resistant HIV protease mutants
ChainB
Resolution1.85 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 1UN B D25 G27 G49 I50 D25 G27 G49 I50 PDBbind-CN: -logKd/Ki=7.57,Kd=27nM
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:2pyn, PDBe:2pyn, PDBj:2pyn
PDBsum2pyn
PubMed17977555
UniProtP03367|POL_HV1BR Gag-Pol polyprotein (Gene Name=gag-pol)

[Back to BioLiP]