› 2ho2

X-ray diffraction
1.33Å resolution

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

Released:
DOI: 10.2210/pdb2ho2/pdb
PDB entry 2ho2 coloured by chain, front view.
PDB entry 2ho2 coloured by chain, side view.
PDB entry 2ho2 coloured by chain, top view.
Source organism: Homo sapiens
Primary publication:
Structural basis for polyproline recognition by the FE65 WW domain.
Meiyappan M, Birrane G, Ladias JAA
J Mol Biol 372 970-980 (2007)
PMID: 17686488

Function and Biology Details

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

Structure analysis Details

Assembly composition:
hetero dimer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-126158 (preferred)
Entry contents:
2 distinct polypeptide molecules
Macromolecules (2 distinct):
Amyloid beta 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:
Ligand GOL 1 x GOL
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

Quick links

Citations

8 review citations

ABL tyrosine kinases: evolution of function, regulation, and specificity.
Colicelli J. (2010)
7 more

13 mentions without citation

Structural and biochemical basis for ubiquitin ligase recruitment by arrestin-related domain-containing protein-3 (ARRDC3).
Qi et al. (2014)
12 more