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Ligands
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F53 (3r,3as,6ar)-hexahydrofuro[2,3-B]furan-3-yl {(1s,2r)-1-benzyl-3-[(2-ethylbutyl){[4-(hydroxymethyl)phenyl]sulfonyl}amino]-2-hydroxypropyl}carbamate
PO4 Phosphate ion
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Code : 3O9G   PDBj   RCSB PDB   PDBe
Header : HYDROLASE/HYDROLASE INHIBITOR
Title : Crystal Structure of wild-type HIV-1 Protease in complex with af53
Release Data : 2011-08-10
Compound :
mol_id molecule chains
1 Protease A,B
fragment: HIV-1 protease (UNP residues 1 to 99)
mutation: Q7K
Source :
mol_id organism_scientific organism_common expression_system
1 Human immunodeficiency virus 1  (taxid:11676) HIV-1 Escherichia coli  (taxid:562)
strain: HXB2
gene: gag-pol, pol
expression_system_strain: TAP106
expression_system_vector_type: plasmid
expression_system_plasmid: pXC35
Authors : Schiffer, C.A., Nalam, M.N.L.
Keywords : HIV-1 protease, drug resistance, drug design, Protease inhibitors, AIDS, Aspartyl protease, HYDROLASE-HYDROLASE INHIBITOR complex
Exp. method : X-RAY DIFFRACTION ( 1.65 Å )
Citation :

Substrate envelope-designed potent HIV-1 protease inhibitors to avoid drug resistance.

Nalam, M.N.,Ali, A.,Reddy, G.S.  et al.
(2013)  Chem.Biol.  20 : 1116 - 1124

PubMed: 24012370
DOI: 10.1016/j.chembiol.2013.07.014

Chain : A, B
UniProt : Q90K99 (Q90K99_9HIV1)
Reaction: EC: Evidence:
Physiological Direction:
Endohydrolysis of RNA in RNA/DNA hybrids. Three different cleavage modes: 1. sequence-specific internal cleavage of RNA. Human immunodeficiency virus type 1 and Moloney murine leukemia virus enzymes prefer to cleave the RNA strand one nucleotide away from the RNA-DNA junction. 2. RNA 5'-end directed cleavage 13-19 nucleotides from the RNA end. 3. DNA 3'-end directed cleavage 15-20 nucleotides away from the primer terminus. 3.1.26.13 ARBA:ARBA00023415
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