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3QPJ

HIV-1 protease (mutant Q7K L33I L63I) in complex with a three-armed pyrrolidine-based inhibitor

Functional Information from GO Data
ChainGOidnamespacecontents
A0004190molecular_functionaspartic-type endopeptidase activity
A0006508biological_processproteolysis
B0004190molecular_functionaspartic-type endopeptidase activity
B0006508biological_processproteolysis
Functional Information from PDB Data
site_idAC1
Number of Residues4
DetailsBINDING SITE FOR RESIDUE CL A 100
ChainResidue
ATHR74
AASN88
AHOH160
BARG41

site_idAC2
Number of Residues19
DetailsBINDING SITE FOR RESIDUE N4I B 100
ChainResidue
AGLY48
AILE50
BARG8
BLEU23
BASP25
BALA28
BASP29
BASP30
BGLY48
BGLY49
BILE50
BPRO81
BILE84
BDTD103
AASP25
AGLY27
AALA28
AASP29
AASP30

site_idAC3
Number of Residues3
DetailsBINDING SITE FOR RESIDUE CL B 101
ChainResidue
BTHR74
BASN88
BHOH187

site_idAC4
Number of Residues2
DetailsBINDING SITE FOR RESIDUE CL B 102
ChainResidue
BTRP6
BHOH151

site_idAC5
Number of Residues8
DetailsBINDING SITE FOR RESIDUE DTD B 103
ChainResidue
ALEU23
AASP25
AILE84
BGLY27
BGLY48
BGLY49
BN4I100
BHOH116

Functional Information from PROSITE/UniProt
site_idPS00141
Number of Residues12
DetailsASP_PROTEASE Eukaryotic and viral aspartyl proteases active site. ALLDTGADDTVI
ChainResidueDetails
AALA22-ILE33

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues2
DetailsACT_SITE: For protease activity; shared with dimeric partner => ECO:0000255|PROSITE-ProRule:PRU10094
ChainResidueDetails
AASP25
BASP25

site_idSWS_FT_FI2
Number of Residues2
DetailsSITE: Cleavage; by viral protease => ECO:0000250
ChainResidueDetails
APHE99
BPHE99

226262

PDB entries from 2024-10-16

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