3PSU

HIV-1 protease in complex with an isobutyl decorated oligoamine (symmetric binding mode)

Functional Information from GO Data

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

Functional Information from PDB Data

site_id	AC1
Number of Residues	13
Details	BINDING SITE FOR RESIDUE LJG A 100

Chain	Residue
A	ASP25
A	ILE84
A	HOH108
A	HOH108
A	HOH161
A	ASP25
A	GLY27
A	ASP30
A	VAL32
A	GLY48
A	GLY49
A	ILE50
A	VAL82

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site_id	AC2
Number of Residues	3
Details	BINDING SITE FOR RESIDUE CL A 101

Chain	Residue
A	GLY73
A	THR74
A	ASN88

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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	1
Details	ACT_SITE: For protease activity; shared with dimeric partner => ECO:0000255|PROSITE-ProRule:PRU10094, ECO:0000269|PubMed:12924029

Chain	Residue	Details
A	ASP25

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site_id	SWS_FT_FI2
Number of Residues	1
Details	SITE: Cleavage; by viral protease => ECO:0000269|PubMed:2476069

Chain	Residue	Details
A	PHE99

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