1A9M

G48H MUTANT OF HIV-1 PROTEASE IN COMPLEX WITH A PEPTIDIC INHIBITOR U-89360E

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 U0E B 100

Chain	Residue
A	ARG8
B	GLY27
B	ALA28
B	ASP29
B	ASP30
B	ILE47
B	HIS48
B	GLY49
B	ILE50
B	VAL82
A	ASP25
A	GLY27
A	GLY49
A	VAL82
A	ILE84
A	HOH102
B	LEU23
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, ECO:0000269|PubMed:12924029

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	ILE64
B	ILE64

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site_id	SWS_FT_FI3
Number of Residues	2
Details	SITE: Cleavage; by viral protease => ECO:0000269|PubMed:2476069

Chain	Residue	Details
A	PHE99
B	PHE99

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site_id	SWS_FT_FI4
Number of Residues	2
Details	MOD_RES: Phosphotyrosine; by host => ECO:0000250

Chain	Residue	Details
A	ILE64
B	ILE64

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