Structure of PDB 3spk Chain A

Receptor sequence
>3spkA (length=99) Species: 11676 (Human immunodeficiency virus 1) [Search protein sequence]
PQITLWKRPIVTIKIGGQLKEALLNTGADDTVLEEVNLPGRWKPKLIGGI
GGFVKVRQYDQVPIEICGHKVIGTVLVGPTPTNVIGRNLMTQIGCTLNF
3D structure
PDB3spk The higher barrier of darunavir and tipranavir resistance for HIV-1 protease.
ChainA
Resolution1.24 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) N25 T26 G27
Catalytic site (residue number reindexed from 1) N25 T26 G27
Enzyme Commision number 3.1.26.13: retroviral ribonuclease H.
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 R8 N25 D29 D30 I47 G48 G49 I50 P81 T82 R8 N25 D29 D30 I47 G48 G49 I50 P81 T82 MOAD: ic50=3.02nM
PDBbind-CN: -logKd/Ki=8.52,IC50=3.02nM
BS02 TPV A R8 L23 N25 A28 I50 T82 R8 L23 N25 A28 I50 T82 MOAD: ic50=3.02nM
PDBbind-CN: -logKd/Ki=8.52,IC50=3.02nM
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:3spk, PDBe:3spk, PDBj:3spk
PDBsum3spk
PubMed21871444
UniProtQ000H7

[Back to BioLiP]