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1BDL

HIV-1 (2:31-37) 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 Residues14
DetailsBINDING SITE FOR RESIDUE IM1 A 400
ChainResidue
AGLY49
AHOH500
BARG8
BGLY48
BGLY49
BPHE53
BIM1600
AGLY27
AASP29
AASP30
ALYS45
AMET46
AILE47
AGLY48

site_idAC2
Number of Residues12
DetailsBINDING SITE FOR RESIDUE IM1 B 600
ChainResidue
AARG8
APRO81
AIM1400
AHOH500
BGLY27
BALA28
BASP29
BASP30
BLYS45
BILE47
BGLY48
BILE50

site_idIM1
Number of Residues2
Details
ChainResidue
AASP29
BASP29

Functional Information from PROSITE/UniProt
site_idPS00141
Number of Residues12
DetailsASP_PROTEASE Eukaryotic and viral aspartyl proteases active site. ALLDTGADDSIV
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

Catalytic Information from CSA
site_idCSA1
Number of Residues4
DetailsAnnotated By Reference To The Literature 1a30
ChainResidueDetails
AASP25
ATHR26
BASP25
BTHR26

site_idCSA2
Number of Residues2
DetailsAnnotated By Reference To The Literature 1a30
ChainResidueDetails
AASP25
BASP25

224931

PDB entries from 2024-09-11

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