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4DQF

Crystal Structure of (G16A/L38A) 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 Residues19
DetailsBINDING SITE FOR RESIDUE 017 B 101
ChainResidue
AASP25
AHOH118
BASP25
BGLY27
BALA28
BASP29
BASP30
BGLY48
BGLY49
BILE50
BHOH206
AGLY27
AALA28
AASP30
AGLY48
AGLY49
APRO81
AVAL82
AILE84

site_idAC2
Number of Residues4
DetailsBINDING SITE FOR RESIDUE SO4 B 102
ChainResidue
APRO1
ALYS55
BHIS69
BLYS70

site_idAC3
Number of Residues3
DetailsBINDING SITE FOR RESIDUE SO4 B 103
ChainResidue
BPRO1
BARG57
BHIS69

site_idAC4
Number of Residues6
DetailsBINDING SITE FOR RESIDUE EDO B 104
ChainResidue
ATRP6
AGLY52
BTHR91
BGLY94
BHOH214
BHOH215

site_idAC5
Number of Residues3
DetailsBINDING SITE FOR RESIDUE GOL B 105
ChainResidue
BLYS20
BGLU21
BASN83

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

222415

PDB entries from 2024-07-10

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