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4J5J

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

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 Residues3
DetailsBINDING SITE FOR RESIDUE CL A 101
ChainResidue
BASP135
BGLY178
BPRO179

site_idAC2
Number of Residues20
DetailsBINDING SITE FOR RESIDUE 478 B 401
ChainResidue
AGLY49
AILE50
AVAL82
BASP125
BGLY127
BALA128
BASN130
BILE132
BGLY148
BGLY149
BILE150
BPRO181
BVAL182
BHOH501
AASP25
AGLY27
AALA28
AASP29
AASN30
AGLY48

site_idAC3
Number of Residues17
DetailsBINDING SITE FOR RESIDUE 478 B 402
ChainResidue
ATRP6
AGLY40
AARG41
BTRP142
BPRO144
BLYS145
BLYS155
BVAL156
BARG157
BVAL177
BPRO179
BGLN192
BILE193
BGLY194
BCL404
BHOH508
BHOH545

site_idAC4
Number of Residues1
DetailsBINDING SITE FOR RESIDUE CL B 403
ChainResidue
BGLU121

site_idAC5
Number of Residues2
DetailsBINDING SITE FOR RESIDUE CL B 404
ChainResidue
ATRP6
B478402

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
BASP125

site_idSWS_FT_FI2
Number of Residues2
DetailsSITE: Cleavage; by viral protease => ECO:0000250
ChainResidueDetails
APHE99
BPHE199

221051

PDB entries from 2024-06-12

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