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3NU5

Crystal Structure of HIV-1 Protease Mutant I50V with Antiviral Drug 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 Residues6
DetailsBINDING SITE FOR RESIDUE NA A 501
ChainResidue
AASP60
AHOH1013
AHOH1022
AHOH1066
AHOH1073
AHOH1085

site_idAC2
Number of Residues4
DetailsBINDING SITE FOR RESIDUE CL A 511
ChainResidue
BARG141
ATHR74
AASN88
AHOH1105

site_idAC3
Number of Residues2
DetailsBINDING SITE FOR RESIDUE CL A 517
ChainResidue
AILE54
ALYS55

site_idAC4
Number of Residues7
DetailsBINDING SITE FOR RESIDUE ACT A 802
ChainResidue
AGLN18
AMET36
ASER37
AHOH1033
BTHR112
BGLU165
BACT801

site_idAC5
Number of Residues25
DetailsBINDING SITE FOR RESIDUE 478 B 401
ChainResidue
AASP25
AGLY27
AALA28
AASP29
AASP30
AGLY48
AGLY49
AVAL50
AVAL82
AILE84
AHOH1155
BLEU123
BASP125
BGLY127
BALA128
BASP129
BASP130
BVAL132
BGLY148
BGLY149
BVAL150
BPRO181
BVAL182
BILE184
BHOH1001

site_idAC6
Number of Residues4
DetailsBINDING SITE FOR RESIDUE NA B 502
ChainResidue
BASP160
BHOH1023
BHOH1113
BHOH1177

site_idAC7
Number of Residues6
DetailsBINDING SITE FOR RESIDUE NA B 503
ChainResidue
BHOH1157
BHOH1158
BHOH1159
BHOH1160
BHOH1161
BHOH1162

site_idAC8
Number of Residues1
DetailsBINDING SITE FOR RESIDUE CL B 512
ChainResidue
BTRP106

site_idAC9
Number of Residues3
DetailsBINDING SITE FOR RESIDUE CL B 513
ChainResidue
BTHR174
BASN188
BHOH1025

site_idBC1
Number of Residues2
DetailsBINDING SITE FOR RESIDUE CL B 514
ChainResidue
BTHR112
BHOH1174

site_idBC2
Number of Residues2
DetailsBINDING SITE FOR RESIDUE CL B 515
ChainResidue
BLYS120
BGLU121

site_idBC3
Number of Residues3
DetailsBINDING SITE FOR RESIDUE CL B 516
ChainResidue
BGLN118
BMET136
BSER137

site_idBC4
Number of Residues8
DetailsBINDING SITE FOR RESIDUE ACT B 801
ChainResidue
AACT802
BTHR112
BILE113
BLYS114
BGLU165
BILE166
BALA167
BGLY168

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 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"},{"source":"PubMed","id":"12924029","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

246031

PDB entries from 2025-12-10

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