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3OK9

Crystal structure of wild-type HIV-1 protease with new oxatricyclic designed inhibitor GRL-0519A

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 Residues32
DetailsBINDING SITE FOR RESIDUE G52 A 401
ChainResidue
AARG8
AILE50
APRO81
AVAL82
AILE84
AHOH1001
AHOH1026
AHOH1122
AHOH1123
AHOH1160
BARG108
AASP25
BASP125
BGLY127
BALA128
BASP129
BASP130
BVAL132
BGLY148
BGLY149
BILE150
BPRO181
AGLY27
BVAL182
BILE184
BCL514
AALA28
AASP29
AASP30
AILE47
AGLY48
AGLY49

site_idAC2
Number of Residues4
DetailsBINDING SITE FOR RESIDUE NA A 502
ChainResidue
AASP60
AHOH1107
AHOH1108
AHOH1170

site_idAC3
Number of Residues1
DetailsBINDING SITE FOR RESIDUE CL A 512
ChainResidue
ATRP6

site_idAC4
Number of Residues3
DetailsBINDING SITE FOR RESIDUE CL A 516
ChainResidue
ATHR74
AASN88
AHOH1016

site_idAC5
Number of Residues5
DetailsBINDING SITE FOR RESIDUE GOL A 601
ChainResidue
ATRP42
ALYS55
AARG57
AHOH1151
AHOH1152

site_idAC6
Number of Residues6
DetailsBINDING SITE FOR RESIDUE NA B 501
ChainResidue
BASP160
BHOH1002
BHOH1003
BHOH1004
BHOH1005
BHOH1006

site_idAC7
Number of Residues4
DetailsBINDING SITE FOR RESIDUE CL B 511
ChainResidue
AARG41
BTHR174
BASN188
BHOH1145

site_idAC8
Number of Residues3
DetailsBINDING SITE FOR RESIDUE CL B 513
ChainResidue
BGLN118
BSER137
BHOH1072

site_idAC9
Number of Residues3
DetailsBINDING SITE FOR RESIDUE CL B 514
ChainResidue
AG52401
BILE147
BGLY148

site_idBC1
Number of Residues6
DetailsBINDING SITE FOR RESIDUE CL B 515
ChainResidue
BLYS120
BGLU121
BGLU134
BASN183
BHOH1095
BHOH1175

site_idBC2
Number of Residues7
DetailsBINDING SITE FOR RESIDUE GOL B 602
ChainResidue
AILE54
APRO79
BTHR104
BTRP106
BILE150
BGLY151
BHOH1098

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, ECO:0000269|PubMed:12924029
ChainResidueDetails
AASP25
BASP125

site_idSWS_FT_FI2
Number of Residues2
DetailsSITE: Cleavage; by viral protease => ECO:0000269|PubMed:2476069
ChainResidueDetails
APHE99
BPHE199

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PDB entries from 2024-05-01

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