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1QBT

HIV-1 PROTEASE INHIBITORS WIIH LOW NANOMOLAR POTENCY

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 Residues24
DetailsBINDING SITE FOR RESIDUE 146 B 300
ChainResidue
AASP25
APRO81
AILE84
BARG8
BASP25
BGLY27
BALA28
BASP30
BVAL32
BLYS45
BGLY48
AGLY27
BGLY49
BILE50
BPRO81
BPRO81
BILE84
AALA28
AASP30
AVAL32
AILE47
AGLY48
AGLY49
AILE50

Functional Information from PROSITE/UniProt
site_idPS00141
Number of Residues12
DetailsASP_PROTEASE Eukaryotic and viral aspartyl proteases active site. ALLDTGADDTVL
ChainResidueDetails
AALA22-LEU33

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues2
DetailsSITE: Cleavage; by viral protease => ECO:0000250
ChainResidueDetails
ALEU76
BLEU76

site_idSWS_FT_FI2
Number of Residues2
DetailsMOD_RES: Phosphotyrosine; by host => ECO:0000250
ChainResidueDetails
ALEU76
BLEU76

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

site_idMCSA1
Number of Residues
DetailsM-CSA 175
ChainResidueDetails

site_idMCSA2
Number of Residues
DetailsM-CSA 175
ChainResidueDetails

227111

PDB entries from 2024-11-06

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