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1BDR

HIV-1 (2: 31, 33-37) PROTEASE COMPLEXED WITH INHIBITOR SB203386

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 Residues16
DetailsBINDING SITE FOR RESIDUE IM1 B 400
ChainResidue
AVAL82
BASP25
BGLY27
BALA28
BASP29
BGLY48
BGLY49
BILE50
BHOH525
AARG8
AASP25
AGLY27
AALA28
AASP29
AGLY48
AGLY49

site_idIM1
Number of Residues2
DetailsIM1 BINDING SITE.
ChainResidue
AASP29
BASP29

Functional Information from PROSITE/UniProt
site_idPS00141
Number of Residues12
DetailsASP_PROTEASE Eukaryotic and viral aspartyl proteases active site. ALLDTGADDSVV
ChainResidueDetails
AALA22-VAL33

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues2
DetailsSITE: Cleavage; by viral protease => ECO:0000250
ChainResidueDetails
AILE64
BILE64

site_idSWS_FT_FI2
Number of Residues2
DetailsMOD_RES: Phosphotyrosine; by host => ECO:0000250
ChainResidueDetails
AILE64
BILE64

218853

PDB entries from 2024-04-24

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