› 1goa

X-ray diffraction
1.9Å resolution

COOPERATIVE STABILIZATION OF ESCHERICHIA COLI RIBONUCLEASE HI BY INSERTION OF GLY-80B AND GLY-77-> ALA SUBSTITUTION

Released:
DOI: 10.2210/pdb1goa/pdb
PDB entry 1goa coloured by chain, front view.
PDB entry 1goa coloured by chain, side view.
PDB entry 1goa coloured by chain, top view.
Source organism: Escherichia coli
Primary publication:
Cooperative stabilization of Escherichia coli ribonuclease HI by insertion of Gly-80b and Gly-77-->Ala substitution.
Ishikawa K, Nakamura H, Morikawa K, Kimura S, Kanaya S
Biochemistry 32 7136-42 (1993)
PMID: 8393706

Function and Biology Details

Reaction catalysed: 
Endonucleolytic cleavage to 5'-phosphomonoester.
Biochemical function:
Biological process:
  • not assigned
Cellular component:
  • not assigned
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: 156 amino acids
Theoretical weight: 17.68 KDa
Source organism: Escherichia coli
Expression system: Not provided
UniProt:
  • Canonical: P0A7Y4 (Residues: 1-80, 81-155; 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: 45.03Å b: 86.93Å c: 35.04Å
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

2 review citations

Helix capping.
Aurora et al. (1998)
1 more

5 mentions without citation

Validating Molecular Dynamics Simulations against Experimental Observables in Light of Underlying Conformational Ensembles.
Childers et al. (2018)
4 more