› 1enh

X-ray diffraction
2.1Å resolution

STRUCTURAL STUDIES OF THE ENGRAILED HOMEODOMAIN

Released:
DOI: 10.2210/pdb1enh/pdb
PDB entry 1enh coloured by chain, front view.
PDB entry 1enh coloured by chain, side view.
PDB entry 1enh coloured by chain, top view.
Source organism: Drosophila melanogaster
Primary publication:
Structural studies of the engrailed homeodomain.
Clarke ND, Kissinger CR, Desjarlais J, Gilliland GL, Pabo CO
Protein Sci 3 1779-87 (1994)
PMID: 7849596

Function and Biology Details

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

Structure analysis Details

Assembly composition:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-526992 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Segmentation polarity homeobox protein engrailed Chain: A
Molecule details ›
Chain: A
Length: 54 amino acids
Theoretical weight: 6.62 KDa
Source organism: Drosophila melanogaster
Expression system: Not provided
UniProt:
  • Canonical: P02836 (Residues: 456-509; Coverage: 10%)
Gene names: CG9015, en
Sequence domains: Homeodomain
Structure domains: Homeodomain-like

Ligands and Environments

No bound ligands
No modified residues

Experiments and Validation Details

Entry percentile scores
Spacegroup: P6522
Unit cell:
a: 44.67Å b: 44.67Å c: 118.12Å
α: 90° β: 90° γ: 120°
R-values:
R R work R free
0.197 0.197 not available
Expression system: Not provided

Quick links

Citations

10 review citations

Is there a unifying mechanism for protein folding?
Daggett et al. (2003)
9 more

96 mentions without citation

Polarizable atomic multipole solutes in a Poisson-Boltzmann continuum.
Schnieders et al. (2007)
95 more