› 1eh2

Solution NMR

STRUCTURE OF THE SECOND EPS15 HOMOLOGY DOMAIN OF HUMAN EPS15, NMR, 20 STRUCTURES

Released:
DOI: 10.2210/pdb1eh2/pdb
PDB entry 1eh2 coloured by chain, ensemble of 20 models, front view.
PDB entry 1eh2 coloured by chain, ensemble of 20 models, side view.
PDB entry 1eh2 coloured by chain, ensemble of 20 models, top view.
Source organism: Homo sapiens
Primary publication:
Structure and Asn-Pro-Phe binding pocket of the Eps15 homology domain.
de Beer T, Carter RE, Lobel-Rice KE, Sorkin A, Overduin M
Science 281 1357-60 (1998)
PMID: 9721102

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-154663 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Epidermal growth factor receptor substrate 15 Chain: A
Molecule details ›
Chain: A
Length: 106 amino acids
Theoretical weight: 11.94 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
UniProt:
  • Canonical: P42566 (Residues: 121-219; Coverage: 11%)
Gene names: AF1P, EPS15
Structure domains: EF-hand

Ligands and Environments

1 bound ligand:
Ligand CA 1 x CA
No modified residues

Experiments and Validation Details

Entry percentile scores
Refinement method: simulated annealing
Expression system: Escherichia coli

Quick links

Citations

24 review citations

Ubiquitin-binding domains.
Hicke et al. (2005)
23 more

18 mentions without citation

OPUS-PSP: an orientation-dependent statistical all-atom potential derived from side-chain packing.
Lu et al. (2008)
17 more