PDBe 1inz

Solution NMR

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

Released:
Source organism: Homo sapiens
Primary publication:
Solution structure of the epsin N-terminal homology (ENTH) domain of human epsin.
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
Structure domain:

Structure analysis Details

Assembly composition:
monomeric (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
Chemical shift assignment: 86%
Refinement method: simulated annealing
Chemical shifts: BMR4959  
Expression system: Escherichia coli BL21