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Solution NMR

Embryonic Neural Inducing Factor Churchill is not a DNA-Binding Zinc Finger Protein: Solution Structure Reveals a Solvent-Exposed beta-Sheet and Zinc Binuclear Cluster

Released:
DOI: 10.2210/pdb2jox/pdb
PDB 2jox coloured by chain and viewed from the front.
PDB 2jox coloured by chain and viewed from the side.
PDB 2jox coloured by chain and viewed from the top.
Source organism: Homo sapiens
Primary publication:
Embryonic neural inducing factor churchill is not a DNA-binding zinc finger protein: solution structure reveals a solvent-exposed beta-sheet and zinc binuclear cluster.
Lee BM, Buck-Koehntop BA, Martinez-Yamout MA, Dyson HJ, Wright PE
J. Mol. Biol. 371 1274-89 (2007)
PMID: 17610897

Function and Biology Details

Biochemical function:
Biological process:
Cellular component:
  • not assigned
Sequence domains:

Structure analysis Details

Assembly composition:
monomeric (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Protein Churchill Chain: A
Molecule details ›
Chain: A
Length: 106 amino acids
Theoretical weight: 12.16 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
UniProt:
  • Canonical: Q8WUH1 (Residues: 29-134; Coverage: 76%)
Gene names: C14orf52, CHCH, CHURC1, My015
Structure domains: Transcription activator, Churchill

Ligands and Environments

1 bound ligand:
Ligand ZN 3 x ZN
No modified residues

Experiments and Validation Details

Entry percentile scores
Chemical shift assignment: 93%
Refinement method: torsion angle dynamics, molecular dynamics
Chemical shifts: BMR15208  
Expression system: Escherichia coli

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Citations

1 review citation

Relationship between the architecture of zinc coordination and zinc binding affinity in proteins--insights into zinc regulation.
Kochańczyk et al. (2015)
10 other articles

3 mentions without citation

Persistent homology analysis of protein structure, flexibility, and folding.
Xia et al. (2014)
2 more