› 1rbs

X-ray diffraction
1.8Å resolution

STRUCTURAL STUDY OF MUTANTS OF ESCHERICHIA COLI RIBONUCLEASE HI WITH ENHANCED THERMOSTABILITY

Released:
DOI: 10.2210/pdb1rbs/pdb
PDB entry 1rbs coloured by chain, front view.
PDB entry 1rbs coloured by chain, side view.
PDB entry 1rbs coloured by chain, top view.
Source organism: Escherichia coli
Primary publication:
Structural study of mutants of Escherichia coli ribonuclease HI with enhanced thermostability.
Ishikawa K, Kimura S, Kanaya S, Morikawa K, Nakamura H
Protein Eng 6 85-91 (1993)
PMID: 8381958

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: 17.56 KDa
Source organism: Escherichia coli
Expression system: Not provided
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

No bound ligands
No modified residues

Experiments and Validation Details

Entry percentile scores
Spacegroup: P212121
Unit cell:
a: 43.96Å b: 86.07Å c: 35.56Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.194 not available not available
Expression system: Not provided

Quick links

Citations

3 review citations

Catalytic antibodies: hapten design strategies and screening methods.
Xu et al. (2004)
2 more

1 mention without citation

Structural and functional characterization of an RNase HI domain from the bifunctional protein Rv2228c from Mycobacterium tuberculosis.
Watkins et al. (2010)