› 2vsz

X-ray diffraction
2.3Å resolution

Crystal Structure of the ELMO1 PH domain

Released:
DOI: 10.2210/pdb2vsz/pdb
PDB entry 2vsz coloured by chain, front view.
PDB entry 2vsz coloured by chain, side view.
PDB entry 2vsz coloured by chain, top view.
Source organism: Homo sapiens
Primary publication:
An alpha-helical extension of the ELMO1 pleckstrin homology domain mediates direct interaction to DOCK180 and is critical in Rac signaling.
Komander D, Patel M, Laurin M, Fradet N, Pelletier A, Barford D, Côté JF
Mol Biol Cell 19 4837-51 (2008)
PMID: 18768751

Function and Biology Details

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

Structure analysis Details

Assembly composition:
homo tetramer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-187689 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Engulfment and cell motility protein 1 Chains: A, B
Molecule details ›
Chains: A, B
Length: 149 amino acids
Theoretical weight: 17.1 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: Q92556 (Residues: 532-675; Coverage: 20%)
Gene names: ELMO1, KIAA0281
Sequence domains: Pleckstrin homology domain
Structure domains:

Ligands and Environments

No bound ligands
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: ESRF BEAMLINE ID23-2
Spacegroup: P6122
Unit cell:
a: 166.016Å b: 166.016Å c: 81.704Å
α: 90° β: 90° γ: 120°
R-values:
R R work R free
0.209 0.208 0.239
Expression system: Escherichia coli BL21(DE3)

Quick links

Citations

11 review citations

I'm coming to GEF you: Regulation of RhoGEFs during cell migration.
Goicoechea et al. (2014)
10 more

5 mentions without citation

An alpha-helical extension of the ELMO1 pleckstrin homology domain mediates direct interaction to DOCK180 and is critical in Rac signaling.
Komander et al. (2008)
4 more