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4DQH

Crystal Structure of (R14C/E65C) HIV-1 Protease in complex with DRV

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 017 B 101
ChainResidue
AASP25
AILE84
BASP25
BGLY27
BALA28
BASP29
BASP30
BGLY48
BILE50
BHOH223
AGLY27
AALA28
AASP30
AVAL32
AGLY48
AGLY49
APRO81
AVAL82

site_idAC2
Number of Residues1
DetailsBINDING SITE FOR RESIDUE GOL B 102
ChainResidue
ALYS55

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

220472

PDB entries from 2024-05-29

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