› 1ovq

Solution NMR

Solution structure of the hypothetical protein YqgF from Escherichia coli

Released:
DOI: 10.2210/pdb1ovq/pdb
PDB entry 1ovq coloured by chain, ensemble of 25 models, front view.
PDB entry 1ovq coloured by chain, ensemble of 25 models, side view.
PDB entry 1ovq coloured by chain, ensemble of 25 models, top view.
Source organism: Escherichia coli
Primary publication:
Solution structure of the hypothetical protein YqgF from Escherichia coli reveals an RNAse H fold.
Liu D, Wang YS, Wyss DF
J Biomol NMR 27 389-92 (2003)
PMID: 14512736

Function and Biology Details

Biochemical function:
Biological process:
Cellular component:
Sequence domains:
Structure domain:

Structure analysis Details

Assembly composition:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-141701 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Putative pre-16S rRNA nuclease Chain: A
Molecule details ›
Chain: A
Length: 138 amino acids
Theoretical weight: 15.21 KDa
Source organism: Escherichia coli
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: P0A8I1 (Residues: 1-138; Coverage: 100%)
Gene names: JW2916, b2949, ruvX, yqgF
Sequence domains: Holliday junction resolvase
Structure domains: YqgF/RNase H-like domain

Ligands and Environments

No bound ligands
No modified residues

Experiments and Validation Details

Entry percentile scores
Refinement method: simulated annealing
Expression system: Escherichia coli BL21(DE3)

Quick links

Citations

1 review citation

RNA damage in biological conflicts and the diversity of responding RNA repair systems.
Burroughs et al. (2016)
9 other articles

1 mention without citation

Biochemical and Structural Study of RuvC and YqgF from Deinococcus radiodurans.
Sun et al. (2022)