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1A30

HIV-1 PROTEASE COMPLEXED WITH A TRIPEPTIDE 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 Residues15
DetailsBINDING SITE FOR CHAIN C OF TRIPEPTIDE GLU-ASP-LEU
ChainResidue
AASP25
BARG8
BASP25
BVAL82
CHOH1075
CHOH1092
CHOH1097
AGLY27
AALA28
AASP29
AASP30
AILE47
AGLY48
AILE50
AHOH1076

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
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 Residues2
Detailsa catalytic site defined by CSA, PubMed 8780786, 11410934
ChainResidueDetails
AASP25
BASP25

site_idMCSA1
Number of Residues
DetailsM-CSA 175
ChainResidueDetails

site_idMCSA2
Number of Residues
DetailsM-CSA 175
ChainResidueDetails

219140

PDB entries from 2024-05-01

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