Brand  (β version)

PDB ID: 2HS2

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Ligands
Code Name Style Show Link
017 (3r,3as,6ar)-hexahydrofuro[2,3-B]furan-3-yl(1s,2r)-3-[[(4-aminophenyl)sulfonyl](isobutyl)amino]-1-benzyl-2-hydroxypropylcarbamate PoSSuM
CL Chloride ion PoSSuM
DMS Dimethyl sulfoxide PoSSuM
Non-standard Residues
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Structure summary

Code : 2HS2   PDBj   RCSB PDB   PDBe
Header : HYDROLASE
Title : Crystal structure of M46L mutant of HIV-1 protease complexed with TMC114 (darunavir)
Release Data : 2006-10-03
Compound :
mol_id molecule chains synonym
1 protease A,B Retropepsin, PR
ec: 3.4.23.16
fragment: HIV-1 protease (residues 500-598)
mutation: Q7K, L33I, M46L, L63I, C67A, C95A
Source :
mol_id organism_scientific expression_system
1 Human immunodeficiency virus 1  (taxid:11676) Escherichia coli  (taxid:562)
gene: GAG
Authors : Weber, I.T., Kovalevsky, A.Y., Liu, F.
Keywords : aspartic protease active site surface binding site, HYDROLASE
Exp. method : X-RAY DIFFRACTION ( 1.22 Å )
Citation :

Ultra-high Resolution Crystal Structure of HIV-1 Protease Mutant Reveals Two Binding Sites for Clinical Inhibitor TMC114.

Kovalevsky, A.Y.,Liu, F.,Leshchenko, S.  et al.
(2006)  J.Mol.Biol.  363 : 161 - 173

PubMed: 16962136
DOI: 10.1016/j.jmb.2006.08.007

Reaction

Chain : A, B
UniProt : P03368 (POL_HV1B1)
Reaction: EC: Evidence:
Physiological Direction:
Specific for a P1 residue that is hydrophobic, and P1' variable, but often Pro. 3.4.23.16 PROSITE-ProRule:PRU00275
-
3'-end directed exonucleolytic cleavage of viral RNA-DNA hybrid. 3.1.13.2 ECO:0000250
-
[Reverse transcriptase/ribonuclease H]
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 PubMed:2476069
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[Reverse transcriptase/ribonuclease H]
DNA(n) + a 2'-deoxyribonucleoside 5'-triphosphate = DNA(n+1) + diphosphate 		2.7.7.49 PROSITE-ProRule:PRU00405, PubMed:2476069
-
[Reverse transcriptase/ribonuclease H]
DNA(n) + a 2'-deoxyribonucleoside 5'-triphosphate = DNA(n+1) + diphosphate 		2.7.7.7 PROSITE-ProRule:PRU00405, PubMed:2476069
-
Cofactor: Evidence: Note:
Mg(2+) ECO:0000250
Binds 2 magnesium ions for reverse transcriptase polymerase activity.
Mg(2+) ECO:0000250
Binds 2 magnesium ions for ribonuclease H (RNase H) activity. Substrate-binding is a precondition for magnesium binding.
Mg(2+) ECO:0000250
Magnesium ions are required for integrase activity. Binds at least 1, maybe 2 magnesium ions.