› 7vsa

X-ray diffraction
1.76Å resolution

E. coli Ribonuclease HI in complex with two Mg2+

Released:
DOI: 10.2210/pdb7vsa/pdb
Model geometry
Fit model/data
PDB entry 7vsa coloured by chain, front view.
PDB entry 7vsa coloured by chain, side view.
PDB entry 7vsa coloured by chain, top view.
Source organism: Escherichia coli K-12
Primary publication:
Pivotal role of a conserved histidine in Escherichia coli ribonuclease HI as proposed by X-ray crystallography.
Liao Z, Oyama T, Kitagawa Y, Katayanagi K, Morikawa K, Oda M
OpenAccess logo Acta Crystallogr D Struct Biol 78 390-398 (2022)
PMID: 35234152

Function and Biology Details

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

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 Chains: A, B
Molecule details ›
Chains: A, B
Length: 155 amino acids
Theoretical weight: 17.62 KDa
Source organism: Escherichia coli K-12
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

Ligands and Environments

3 bound ligands:
Ligand GOL 2 x GOL
Ligand MG 4 x MG
Ligand SO4 3 x SO4
No modified residues

Experiments and Validation Details

wwPDB Validation report is not available for this entry.
X-ray source: SPRING-8 BEAMLINE BL45XU
Spacegroup: P2221
Unit cell:
a: 61.639Å b: 64.288Å c: 80.288Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.202 0.2 0.233
Expression system: Escherichia coli

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Citations

1 citations in other articles

Verification: model-free phasing with enhanced predicted models in ARCIMBOLDO_SHREDDER.
Medina et al. (2022)

1 mention without citation

Pivotal role of a conserved histidine in Escherichia coli ribonuclease HI as proposed by X-ray crystallography.
Liao et al. (2022)