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3A2O

Crystal Structure of HIV-1 Protease Complexed with KNI-1689

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 Residues15
DetailsBINDING SITE FOR RESIDUE GOL B 803
ChainResidue
AGLN18
BGLY168
BHOH1477
BHOH1643
BHOH1644
BHOH1645
BHOH1646
AMET36
ASER37
BTHR112
BILE113
BLYS114
BGLU165
BILE166
BALA167

site_idAC2
Number of Residues42
DetailsBINDING SITE FOR RESIDUE KNJ B 999
ChainResidue
ALEU23
AASP25
AGLY27
AALA28
AASP29
AASP30
AVAL32
AGLY48
AGLY49
AILE50
AVAL82
AILE84
AHOH1039
AHOH1433
AHOH1445
AHOH1598
AHOH1638
AHOH1639
AHOH1648
AHOH1657
BLEU123
BASP125
BGLY127
BALA128
BASP129
BASP130
BVAL132
BILE147
BGLY148
BGLY149
BILE150
BPRO181
BILE184
BHOH1079
BHOH1095
BHOH1472
BHOH1568
BHOH1571
BHOH1595
BHOH1596
BHOH1654
BHOH1655

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

237735

PDB entries from 2025-06-18

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