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3UCB

Crystal Structure of Multidrug Resistant HIV-1 Protease Clinical Isolate PR20 in Complex with Darunavir

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 Residues28
DetailsBINDING SITE FOR RESIDUE 017 A 201
ChainResidue
AARG8
AILE50
APRO81
AVAL82
AHOH1065
AHOH1098
BARG8
BASP25
BGLY27
BALA28
BASP29
AASP25
BASN30
BILE32
BGLY48
BGLY49
BILE50
BPRO81
BVAL82
BHOH1045
BHOH1100
AGLY27
AALA28
AASP29
AASN30
AILE32
AGLY48
AGLY49

site_idAC2
Number of Residues21
DetailsBINDING SITE FOR RESIDUE 017 B 202
ChainResidue
ATRP6
AGLY40
AARG41
BTRP42
BPRO44
BLYS45
BLYS55
BVAL56
BARG57
BALA67
BGLY68
BVAL77
BGLY78
BPRO79
BGLN92
BILE93
BGLY94
BHOH1026
BHOH1056
BHOH1086
BHOH1102

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

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

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PDB entries from 2024-07-10

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