8ESY

D30N mutant HIV protease in complex with benzoxaborolone analog of darunavir

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 PROSITE/UniProt

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

Chain	Residue	Details
A	ALA22-ILE33

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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:0000305|PubMed:33542150

Chain	Residue	Details
A	ASP25
B	ASP125

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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	PHE199

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Catalytic Information from CSA

site_id	MCSA1
Number of Residues	3
Details	M-CSA 175

Chain	Residue	Details
A	ASP25	hydrogen bond acceptor, hydrogen bond donor, proton acceptor, proton donor
A	THR26	electrostatic stabiliser, transition state stabiliser
A	GLY27	electrostatic stabiliser, hydrogen bond donor

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site_id	MCSA2
Number of Residues	3
Details	M-CSA 175

Chain	Residue	Details
B	ASP125	hydrogen bond acceptor, hydrogen bond donor, proton acceptor, proton donor
B	THR126	electrostatic stabiliser, transition state stabiliser
B	GLY127	electrostatic stabiliser, hydrogen bond donor

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