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3GI0

Crystal structure of a chemically synthesized 203 amino acid 'covalent dimer' [l-ala51,d-ala51'] hiv-1 protease molecule complexed with jg-365 inhibitor

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 Residues7
DetailsBINDING SITE FOR RESIDUE DAL A 155
ChainResidue
AALA51
APHE53
AILE54
AGLY153
AILE154
AGLY156
AHOH263

site_idAC2
Number of Residues7
DetailsBINDING SITE FOR RESIDUE DAL B 155
ChainResidue
BGLY52
BPHE53
BGLY153
BILE154
BGLY156
AHOH259
BALA51

site_idAC3
Number of Residues20
DetailsBINDING SITE FOR CHAIN C OF JG-365 INHIBITOR
ChainResidue
AARG8
AASP25
AGLY27
AALA28
AASP29
AASP30
AILE47
AGLY48
AGLY49
AILE50
AARG112
AASP129
AGLY131
AALA132
AASP133
AGLY152
AGLY153
APRO185
AVAL186
AHOH207

site_idAC4
Number of Residues20
DetailsBINDING SITE FOR CHAIN D OF JG-365 INHIBITOR
ChainResidue
AHOH207
BARG8
BASP25
BGLY27
BALA28
BASP29
BASP30
BILE47
BGLY48
BGLY49
BILE50
BILE84
BASP129
BGLY131
BASP133
BGLY152
BGLY153
BILE154
BPRO185
BILE188

Functional Information from PROSITE/UniProt
site_idPS00141
Number of Residues12
DetailsASP_PROTEASE Eukaryotic and viral aspartyl proteases active site. ALLDTGADDTVI
ChainResidueDetails
AALA22-ILE33
AALA126-ILE137

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
AASP129
BASP129

site_idSWS_FT_FI2
Number of Residues2
DetailsSITE: Cleavage; by viral protease => ECO:0000250
ChainResidueDetails
APHE203
BPHE203

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PDB entries from 2024-07-24

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