Structure of PDB 2o4l Chain A

Receptor sequence
>2o4lA (length=99) Species: 11676 (Human immunodeficiency virus 1) [Search protein sequence]
PQITLWKRPLVTIKIGGQLKEALLDTGADDTVLEEMSLPGRWKPKMIGGV
GGFIKVRQYDQILIEICGHKAIGTVLVGPTPVNIIGRNLLTQIGCTLNF
3D structure
PDB2o4l Unique thermodynamic response of tipranavir to human immunodeficiency virus type 1 protease drug resistance mutations.
ChainA
Resolution1.33 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 ?
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 TPV A D25 G27 A28 D29 D30 G48 V50 P81 D25 G27 A28 D29 D30 G48 V50 P81 MOAD: Kd=608pM
PDBbind-CN: -logKd/Ki=9.22,Kd=608pM
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:2o4l, PDBe:2o4l, PDBj:2o4l
PDBsum2o4l
PubMed17360759
UniProtQ1G1C3

[Back to BioLiP]