› 1g15

X-ray diffraction
1.9Å resolution

CO-CRYSTAL OF E. COLI RNASE HI WITH TWO MN2+ IONS BOUND IN THE THE ACTIVE SITE

Released:
DOI: 10.2210/pdb1g15/pdb
PDB entry 1g15 coloured by chain, front view.
PDB entry 1g15 coloured by chain, side view.
PDB entry 1g15 coloured by chain, top view.
Source organism: Escherichia coli
Primary publication:
Co-crystal of Escherichia coli RNase HI with Mn2+ ions reveals two divalent metals bound in the active site.
Goedken ER, Marqusee S
J Biol Chem 276 7266-71 (2001)
PMID: 11083878

Function and Biology Details

Reaction catalysed: 
Endonucleolytic cleavage to 5'-phosphomonoester.
Biochemical function:
Biological process:
Cellular component:
Sequence domains:
Structure domain:

Structure analysis Details

Assembly composition:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-141635 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Ribonuclease HI Chain: A
Molecule details ›
Chain: A
Length: 155 amino acids
Theoretical weight: 17.47 KDa
Source organism: Escherichia coli
Expression system: Escherichia coli
UniProt:
  • Canonical: P0A7Y4 (Residues: 1-155; Coverage: 100%)
Gene names: JW0204, b0214, dasF, herA, rnh, rnhA, sdrA
Sequence domains: RNase H
Structure domains: Ribonuclease H-like superfamily/Ribonuclease H

Ligands and Environments

1 bound ligand:
Ligand MN 2 x MN
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: ALS BEAMLINE 5.0.2
Spacegroup: P63
Unit cell:
a: 71.653Å b: 71.653Å c: 48.127Å
α: 90° β: 90° γ: 120°
R-values:
R R work R free
0.223 0.223 0.261
Expression system: Escherichia coli

Quick links

Citations

7 review citations

Making and breaking nucleic acids: two-Mg2+-ion catalysis and substrate specificity.
Yang et al. (2006)
6 more

9 mentions without citation

RNA sequencing by direct tagmentation of RNA/DNA hybrids.
Di et al. (2020)
8 more