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3D20

Crystal structure of HIV-1 mutant I54V and inhibitor DARUNAVIA

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 Residues1
DetailsBINDING SITE FOR RESIDUE NA A 901
ChainResidue
AASP60

site_idAC2
Number of Residues3
DetailsBINDING SITE FOR RESIDUE CL A 903
ChainResidue
ATHR74
AASN88
BARG141

site_idAC3
Number of Residues22
DetailsBINDING SITE FOR RESIDUE 017 A 201
ChainResidue
AASP29
AASP30
AGLY48
AGLY49
AILE50
APRO81
AILE84
BASP125
BGLY127
BALA128
BASP129
BASP130
BGLY148
BGLY149
BILE150
BPRO181
BILE184
AARG8
ALEU23
AASP25
AGLY27
AALA28

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
BASP125

site_idSWS_FT_FI2
Number of Residues2
DetailsSITE: Cleavage; by viral protease => ECO:0000250
ChainResidueDetails
APHE99
BPHE199

220113

PDB entries from 2024-05-22

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