Brand  (β version)

PDB ID: 3K2P

Hetero Atom Contents

  The number of atoms exceeds 100,000.
  So, it can not be displayed here.

Select unit:

Select hetatm:   

close
information
centroid:
interaction residue:

Select chain:   Sequence  

Data format:   

Color scheme of protein:

Ligands
Code Name Style Show Link
MN Manganese (II) ion PoSSuM
JTH 2,7-dihydroxy-4-(propan-2-yl)cyclohepta-2,4,6-trien-1-one PoSSuM
Non-standard Residues
Code Name Show
Glycosylation
Code Name Emphasize
Modification
Code Name Show

Structure summary

Code : 3K2P   PDBj   RCSB PDB   PDBe
Header : HYDROLASE
Title : HIV-1 Reverse Transcriptase Isolated RnaseH Domain with the Inhibitor beta-thujaplicinol Bound at the Active Site
Release Data : 2010-02-09
Compound :
mol_id molecule chains synonym
1 Reverse Transcriptase A,B Reverse transcriptase/ribonuclease H, p66 RT
ec: 3.1.26.4
Source :
mol_id organism_scientific organism_common expression_system
1 Human immunodeficiency virus type 1  (taxid:11678) HIV-1 Escherichia coli  (taxid:562)
strain: BH10
gene: gag-pol
expression_system_vector_type: Plasmid
Authors : Pauly, T.A., Himmel, D.M., Maegley, K., Arnold, E.
Keywords : RNAse H inhibitor, reverse transcriptase, AIDS, HIV, protein-inhibitor complex, structure-based drug design, tropolones, tropylium ion, divalent cation chelator, metal-binding, RNA-binding, hydrolase
Exp. method : X-RAY DIFFRACTION ( 2.04 Å )
Citation :

Structure of HIV-1 reverse transcriptase with the inhibitor beta-Thujaplicinol bound at the RNase H active site.

Himmel, D.M.,Maegley, K.A.,Pauly, T.A.  et al.
(2009)  Structure  17 : 1625 - 1635

PubMed: 20004166
DOI: 10.1016/j.str.2009.09.016

Reaction

Chain : A, B
UniProt : P03366 (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
-
[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.