1AZ5

UNLIGANDED SIV PROTEASE STRUCTURE IN AN "OPEN" CONFORMATION

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	NUL
Number of Residues	1
Details	CATALYTIC ASPARTIC ACID.

Chain	Residue
A	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. VLLDTGADDSIV

Chain	Residue	Details
A	VAL22-VAL33

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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

Chain	Residue	Details
A	ASP25

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site_id	SWS_FT_FI2
Number of Residues	3
Details	SITE: Cleavage; by viral protease => ECO:0000250

Chain	Residue	Details
A	ASP30
A	PHE3
A	PHE99

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Catalytic Information from CSA

site_id	CSA1
Number of Residues	2
Details	Annotated By Reference To The Literature 1a30

Chain	Residue	Details
A	ASP25
A	THR26

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site_id	CSA2
Number of Residues	1
Details	Annotated By Reference To The Literature 1a30

Chain	Residue	Details
A	ASP25

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