8F0F

HIV-1 wild type protease with GRL-110-19A, a chloroacetamide derivative based on Darunavir as P2' group

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. ALLDTGADDTVI

Chain	Residue	Details
A	ALA22-ILE33

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Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI2
Number of Residues	20
Details	Region: {"description":"Dimerization of protease","evidences":[{"source":"PubMed","id":"2162350","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details

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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	ASP25	hydrogen bond acceptor, hydrogen bond donor, proton acceptor, proton donor
B	THR26	electrostatic stabiliser, transition state stabiliser
B	GLY27	electrostatic stabiliser, hydrogen bond donor

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