› 1inz

Solution NMR

SOLUTION STRUCTURE OF THE EPSIN N-TERMINAL HOMOLOGY (ENTH) DOMAIN OF HUMAN EPSIN

Released:
DOI: 10.2210/pdb1inz/pdb
PDB entry 1inz coloured by chain, ensemble of 20 models, front view.
PDB entry 1inz coloured by chain, ensemble of 20 models, side view.
PDB entry 1inz coloured by chain, ensemble of 20 models, top view.
Source organism: Homo sapiens
Primary publication:
Solution structure of the epsin N-terminal homology (ENTH) domain of human epsin.
Koshiba S, Kigawa T, Kikuchi A, Yokoyama S
J Struct Funct Genomics 2 1-8 (2002)
PMID: 12836669

Function and Biology Details

Biochemical function:
  • not assigned
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-195365 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Epsin-1 Chain: A
Molecule details ›
Chain: A
Length: 148 amino acids
Theoretical weight: 17.31 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli BL21
UniProt:
  • Canonical: Q9Y6I3 (Residues: 1-144; Coverage: 25%)
Gene name: EPN1
Sequence domains: ENTH domain
Structure domains: Serine Threonine Protein Phosphatase 5, Tetratricopeptide repeat

Ligands and Environments

No bound ligands
No modified residues

Experiments and Validation Details

Entry percentile scores
Refinement method: simulated annealing
Expression system: Escherichia coli BL21

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Citations

1 review citation

Mechanisms of membrane deformation by lipid-binding domains.
Itoh et al. (2009)
4 other articles

6 mentions without citation

Endocytic adaptors--social networking at the plasma membrane.
Reider et al. (2011)
5 more