› 2nml

X-ray diffraction
1.55Å resolution

Crystal structure of HEF2/ERH at 1.55 A resolution

Released:
DOI: 10.2210/pdb2nml/pdb
PDB entry 2nml coloured by chain, front view.
PDB entry 2nml coloured by chain, side view.
PDB entry 2nml coloured by chain, top view.
Source organism: Homo sapiens
Primary publication:
A 1.55 A resolution X-ray crystal structure of HEF2/ERH and insights into its transcriptional and cell-cycle interaction networks.
Jin T, Guo F, Serebriiskii IG, Howard A, Zhang YZ
Proteins 68 427-37 (2007)
PMID: 17444515

Function and Biology Details

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

Structure analysis Details

Assembly composition:
homo dimer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-160813 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Enhancer of rudimentary homolog Chain: A
Molecule details ›
Chain: A
Length: 104 amino acids
Theoretical weight: 12.27 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
UniProt:
  • Canonical: P84090 (Residues: 1-104; Coverage: 100%)
Gene name: ERH
Sequence domains: Enhancer of rudimentary
Structure domains: Enhancer of rudimentary

Ligands and Environments

No bound ligands
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: APS BEAMLINE 17-ID
Spacegroup: P3121
Unit cell:
a: 53.739Å b: 53.739Å c: 67.448Å
α: 90° β: 90° γ: 120°
R-values:
R R work R free
0.2 0.198 0.238
Expression system: Escherichia coli

Quick links

Citations

3 review citations

The enigmatic ERH protein: its role in cell cycle, RNA splicing and cancer.
Weng et al. (2013)
2 more

3 mentions without citation

The RAGNYA fold: a novel fold with multiple topological variants found in functionally diverse nucleic acid, nucleotide and peptide-binding proteins.
Balaji et al. (2007)
2 more