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3QRM

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 Residues22
DetailsBINDING SITE FOR RESIDUE NK7 A 100
ChainResidue
AASP25
ALEU76
ADTD102
AHOH119
BARG8
BASP25
BALA28
BASP30
BGLY48
BGLY49
BILE50
AGLY27
BPRO81
BVAL82
BILE84
AALA28
AASP29
AASP30
AVAL32
AILE47
AGLY48
AILE50

site_idAC2
Number of Residues4
DetailsBINDING SITE FOR RESIDUE CL A 101
ChainResidue
ATHR74
AASN88
AHOH190
BARG41

site_idAC3
Number of Residues9
DetailsBINDING SITE FOR RESIDUE DTD A 102
ChainResidue
ALEU23
AASP25
AVAL82
AILE84
ANK7100
AHOH144
BGLY27
BGLY48
BILE50

site_idAC4
Number of Residues2
DetailsBINDING SITE FOR RESIDUE CL B 100
ChainResidue
BTHR74
BASN88

site_idAC5
Number of Residues2
DetailsBINDING SITE FOR RESIDUE CL B 101
ChainResidue
BTRP6
BHOH286

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 Residues138
DetailsDomain: {"description":"Peptidase A2","evidences":[{"source":"PROSITE-ProRule","id":"PRU00275","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

site_idSWS_FT_FI2
Number of Residues20
DetailsRegion: {"description":"Dimerization of protease","evidences":[{"source":"UniProtKB","id":"P04585","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

site_idSWS_FT_FI3
Number of Residues2
DetailsActive site: {"description":"For protease activity; shared with dimeric partner","evidences":[{"source":"PROSITE-ProRule","id":"PRU10094","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

246905

PDB entries from 2025-12-31

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