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3JW2

HIV-1 Protease Mutant G86S 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 401
ChainResidue
AARG8
AILE50
APRO81
AVAL82
AILE84
AHOH1065
AHOH1102
BLEU123
BASP125
BGLY127
BALA128
AASP25
BASP129
BASP130
BILE147
BGLY148
BGLY149
BILE150
BPRO181
BVAL182
BILE184
AGLY27
AALA28
AASP29
AASP30
AVAL32
AGLY48
AGLY49

site_idAC2
Number of Residues6
DetailsBINDING SITE FOR RESIDUE NA A 501
ChainResidue
AASP60
AHOH1072
AHOH1074
AHOH1086
AHOH1101
AHOH1107

site_idAC3
Number of Residues3
DetailsBINDING SITE FOR RESIDUE CL B 502
ChainResidue
BTRP106
BLYS155
BHOH1104

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
BASP125

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

Catalytic Information from CSA
site_idCSA1
Number of Residues2
DetailsAnnotated By Reference To The Literature 1a30
ChainResidueDetails
AASP25
ATHR26

site_idCSA2
Number of Residues2
DetailsAnnotated By Reference To The Literature 1a30
ChainResidueDetails
BTHR126
BASP125

site_idCSA3
Number of Residues1
DetailsAnnotated By Reference To The Literature 1a30
ChainResidueDetails
AASP25

site_idCSA4
Number of Residues1
DetailsAnnotated By Reference To The Literature 1a30
ChainResidueDetails
BASP125

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PDB entries from 2024-11-06

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