4QLH

Crystal structure of drug resistant V82S/V1082S HIV-1 Protease

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 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
A	ALA1022-LEU1033

---

Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI2
Number of Residues	10
Details	Region: {"description":"Dimerization of protease","evidences":[{"source":"PubMed","id":"2162350","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details

---

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

---