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4QGI

X-ray crystal structure of HIV-1 protease variant G48T/L89M in complex with Saquinavir

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 Residues18
DetailsBINDING SITE FOR RESIDUE ROC A 101
ChainResidue
AASP25
AHOH218
BARG8
BLEU23
BASP25
BTHR48
BGLY49
BILE50
BPRO81
BILE84
AGLY27
AALA28
AASP29
AASP30
ATHR48
AGLY49
AILE50
AHOH201

site_idAC2
Number of Residues5
DetailsBINDING SITE FOR RESIDUE GOL A 102
ChainResidue
AILE54
APRO79
BTRP42
BILE50
BHOH152

Functional Information from PROSITE/UniProt
site_idPS00141
Number of Residues12
DetailsASP_PROTEASE Eukaryotic and viral aspartyl proteases active site. ALLDTGADDTVL
ChainResidueDetails
AALA22-LEU33

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

239803

PDB entries from 2025-08-06

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