› 4ohw

X-ray diffraction
2.3Å resolution

C. Elegans Clp1 bound to ATP, and Mn2+(ATP-bound state)

Released:
DOI: 10.2210/pdb4ohw/pdb
PDB 4ohw coloured by chain and viewed from the front.
PDB 4ohw coloured by chain and viewed from the side.
PDB 4ohw coloured by chain and viewed from the top.
Source organism: Caenorhabditis elegans
Primary publication:
RNA Specificity and Regulation of Catalysis in the Eukaryotic Polynucleotide Kinase Clp1.
Dikfidan A, Loll B, Zeymer C, Magler I, Clausen T, Meinhart A
Mol. Cell (2014)
PMID: 24813946

Function and Biology Details

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

Structure analysis Details

Assembly composition:
monomeric (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Protein clpf-1 Chain: A
Molecule details ›
Chain: A
Length: 431 amino acids
Theoretical weight: 47.94 KDa
Source organism: Caenorhabditis elegans
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: P52874 (Residues: 1-428; Coverage: 100%)
Gene names: F59A2.4, clpf-1
Sequence domains:
Structure domains:

Ligands and Environments

3 bound ligands:
Ligand ATP 1 x ATP
Ligand MN 1 x MN
Ligand 2PE 1 x 2PE
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: SLS BEAMLINE X10SA
Spacegroup: P31
Unit cell:
a: 99.34Å b: 99.34Å c: 40.8Å
α: 90° β: 90° γ: 120°
R-values:
R R work R free
0.204 0.202 0.241
Expression system: Escherichia coli BL21(DE3)

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Citations

2 review citations

RNA damage in biological conflicts and the diversity of responding RNA repair systems.
Burroughs et al. (2016)
1 more