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3TH9

Crystal Structure of HIV-1 Protease Mutant Q7K V32I L63I with a cyclic sulfonamide 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 Residues20
DetailsBINDING SITE FOR RESIDUE 9Y9 A 100
ChainResidue
AASP25
AVAL82
AILE84
AHOH264
BASP25
BGLY27
BGLY48
BGLY49
BILE50
BVAL82
BHOH232
AGLY27
BHOH263
AALA28
AASP29
AASP30
AGLY48
AGLY49
AILE50
APRO81

site_idAC2
Number of Residues20
DetailsBINDING SITE FOR RESIDUE 9Y9 B 100
ChainResidue
AASP25
AGLY27
AGLY48
AGLY49
AILE50
AVAL82
AILE84
BASP25
BGLY27
BALA28
BASP29
BASP30
BGLY48
BGLY49
BILE50
BPRO81
BVAL82
BILE84
BHOH232
BHOH263

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
BASP25

site_idSWS_FT_FI2
Number of Residues2
DetailsSITE: Cleavage; by viral protease => ECO:0000250
ChainResidueDetails
APHE99
BPHE99

224004

PDB entries from 2024-08-21

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