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6C8X

Wild-type HIV-1 protease in complex with a phenylboronic acid (P2') analog of 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 Residues27
Detailsbinding site for residue BVR A 101
ChainResidue
AASP25
APRO81
AVAL82
AILE84
AHOH207
AHOH220
AHOH241
BASP125
BGLY127
BALA128
BASP129
AGLY27
BASP130
BILE147
BGLY148
BGLY149
BILE150
BPRO181
BVAL182
BILE184
AALA28
AASP29
AASP30
AILE47
AGLY48
AGLY49
AILE50

site_idAC2
Number of Residues4
Detailsbinding site for residue CL A 102
ChainResidue
ATHR74
AASN88
AHOH262
BARG141

site_idAC3
Number of Residues1
Detailsbinding site for residue CL B 201
ChainResidue
BTRP106

site_idAC4
Number of Residues8
Detailsbinding site for residue GOL B 202
ChainResidue
AGLN18
AMET36
ASER37
BTHR112
BGLU165
BALA167
BGLY168
BHOH368

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

224931

PDB entries from 2024-09-11

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