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3NU4

Crystal Structure of HIV-1 Protease Mutant V32I 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 500
ChainResidue
AASP60
AHOH1058
AHOH1082
AHOH1114
AHOH1145
AHOH1180

site_idAC2
Number of Residues3
DetailsBINDING SITE FOR RESIDUE CL A 501
ChainResidue
ATHR74
AASN88
BARG141

site_idAC3
Number of Residues17
DetailsBINDING SITE FOR RESIDUE 478 B 401
ChainResidue
AASP25
AGLY27
AALA28
AASP30
AGLY48
AGLY49
AVAL82
AHOH1047
BASP125
BGLY127
BALA128
BASP129
BASP130
BGLY148
BGLY149
BILE150
BHOH1001

site_idAC4
Number of Residues1
DetailsBINDING SITE FOR RESIDUE CL B 502
ChainResidue
BTRP106

site_idAC5
Number of Residues3
DetailsBINDING SITE FOR RESIDUE CL B 503
ChainResidue
BTHR174
BASN188
BHOH1057

Functional Information from PROSITE/UniProt
site_idPS00141
Number of Residues12
DetailsASP_PROTEASE Eukaryotic and viral aspartyl proteases active site. ALLDTGADDTII
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

242199

PDB entries from 2025-09-24

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