1AAQ

HYDROXYETHYLENE ISOSTERE INHIBITORS OF HUMAN IMMUNODEFICIENCY VIRUS-1 PROTEASE: STRUCTURE-ACTIVITY ANALYSIS USING ENZYME KINETICS, X-RAY CRYSTALLOGRAPHY, AND INFECTED T-CELL ASSAYS

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0004190	molecular_function	aspartic-type endopeptidase activity
A	0006508	biological_process	proteolysis
B	0004190	molecular_function	aspartic-type endopeptidase activity
B	0006508	biological_process	proteolysis

Functional Information from PDB Data

site_id	AC1
Number of Residues	18
Details	BINDING SITE FOR RESIDUE PSI B 100

Chain	Residue
A	ARG8
B	GLY27
B	ALA28
B	ASP29
B	ILE47
B	GLY48
B	GLY49
B	PRO81
B	VAL82
B	HOH101
A	ASP25
A	GLY27
A	ALA28
A	ASP29
A	ASP30
A	GLY48
A	GLY49
B	ASP25

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Functional Information from PROSITE/UniProt

site_id	PS00141
Number of Residues	12
Details	ASP_PROTEASE Eukaryotic and viral aspartyl proteases active site. ALLDTGADDTVL

Chain	Residue	Details
A	ALA22-LEU33

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Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	2
Details	ACT_SITE: For protease activity; shared with dimeric partner => ECO:0000255|PROSITE-ProRule:PRU10094

Chain	Residue	Details
A	ASP25
B	ASP25

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site_id	SWS_FT_FI2
Number of Residues	2
Details	SITE: Cleavage; by viral protease => ECO:0000250

Chain	Residue	Details
A	PHE99
B	PHE99

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