2ho2

X-ray diffraction
1.33Å resolution

Structure of human FE65-WW domain in complex with hMena peptide.

Released:
Source organism: Homo sapiens
Primary publication:
Structural basis for polyproline recognition by the FE65 WW domain.
J. Mol. Biol. 372 970-80 (2007)
PMID: 17686488

Function and Biology Details

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

Structure analysis Details

Assembly composition:
hetero dimer (preferred)
Entry contents:
2 distinct polypeptide molecules
Macromolecules (2 distinct):
Amyloid-beta A4 precursor protein-binding family B member 1 Chain: A
Molecule details ›
Chain: A
Length: 38 amino acids
Theoretical weight: 4.19 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
UniProt:
  • Canonical: O00213 (Residues: 253-289; Coverage: 5%)
Gene names: APBB1, FE65, RIR
Sequence domains: WW domain
Protein enabled homolog Chain: B
Molecule details ›
Chain: B
Length: 10 amino acids
Theoretical weight: 1.01 KDa
Source organism: Homo sapiens
Expression system: Not provided
UniProt:
  • Canonical: Q8N8S7 (Residues: 347-356; Coverage: 2%)
Gene names: ENAH, MENA

Ligands and Environments

1 bound ligand:

No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: NSLS BEAMLINE X12B
Spacegroup: P3121
Unit cell:
a: 41.661Å b: 41.661Å c: 38.633Å
α: 90° β: 90° γ: 120°
R-values:
R R work R free
0.174 0.172 0.214
Expression systems:
  • Escherichia coli
  • Not provided