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3U7S

HIV PR drug resistant patient's variant in complex with darunavir

Replaces:  3GGT
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 Residues16
DetailsBINDING SITE FOR RESIDUE 017 A 201
ChainResidue
AASP25
BASP25
BGLY27
BASP30
BGLY48
BGLY49
BPRO81
BLEU82
AGLY27
AALA28
AASP29
AASP30
AGLY48
AILE50
A017202
AHOH373

site_idAC2
Number of Residues19
DetailsBINDING SITE FOR RESIDUE 017 A 202
ChainResidue
AASP25
AGLY27
AASP30
AILE47
AGLY48
AGLY49
AILE50
APRO81
ALEU82
A017201
AHOH373
AHOH376
BASP25
BGLY27
BALA28
BASP29
BASP30
BGLY49
BILE50

site_idAC3
Number of Residues2
DetailsBINDING SITE FOR RESIDUE BME A 203
ChainResidue
ACYS67
BGLY68

site_idAC4
Number of Residues4
DetailsBINDING SITE FOR RESIDUE BME B 101
ChainResidue
AGLY68
BILE3
BVAL11
BCYS67

Functional Information from PROSITE/UniProt
site_idPS00141
Number of Residues12
DetailsASP_PROTEASE Eukaryotic and viral aspartyl proteases active site. ALLDTGADDTIF
ChainResidueDetails
AALA22-PHE33

Functional Information from SwissProt/UniProt
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

246704

PDB entries from 2025-12-24

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