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3T3C

Structure of HIV PR resistant patient derived mutant (comprising 22 mutations) in complex with DRV

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 Residues19
DetailsBINDING SITE FOR RESIDUE 017 A 201
ChainResidue
AASP25
BASP25
BGLY27
BALA28
BASP30
BVAL32
BALA48
BGLY49
BILE50
BALA82
BHOH161
AGLY27
AALA28
AASP29
AASP30
AALA48
AGLY49
AILE50
AHOH103

site_idAC2
Number of Residues1
DetailsBINDING SITE FOR RESIDUE BME A 100
ChainResidue
ACYS67

site_idAC3
Number of Residues5
DetailsBINDING SITE FOR RESIDUE SO4 A 101
ChainResidue
AARG8
AVAL22
ALEU23
AALA82
AASN83

site_idAC4
Number of Residues1
DetailsBINDING SITE FOR RESIDUE BME B 100
ChainResidue
BCYS67

site_idAC5
Number of Residues7
DetailsBINDING SITE FOR RESIDUE SO4 B 101
ChainResidue
BGLU21
BVAL22
BLEU23
BALA82
BASN83
BHOH120
BHOH147

Functional Information from PROSITE/UniProt
site_idPS00141
Number of Residues12
DetailsASP_PROTEASE Eukaryotic and viral aspartyl proteases active site. VLLDTGADDTVI
ChainResidueDetails
AVAL22-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

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PDB entries from 2025-06-18

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