3sog

X-ray diffraction
2.3Å resolution

Crystal structure of the BAR domain of human Amphiphysin, isoform 1

Released:
Source organism: Homo sapiens
Entry authors: Allerston CK, Krojer T, Chaikuad A, Cooper CDO, Berridge G, Savitsky P, Vollmar M, von Delft F, Arrowsmith CH, Weigelt J, Edwards A, Bountra C, Gileadi O, Structural Genomics Consortium (SGC)

Function and Biology Details

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

Structure analysis Details

Assembly composition:
homo dimer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-155945 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Amphiphysin Chain: A
Molecule details ›
Chain: A
Length: 205 amino acids
Theoretical weight: 24.22 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
UniProt:
  • Canonical: P49418 (Residues: 34-236; Coverage: 29%)
Gene names: AMPH, AMPH1
Sequence domains: BAR domain
Structure domains: Arfaptin homology (AH) domain/BAR domain

Ligands and Environments

2 bound ligands:
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: DIAMOND BEAMLINE I04-1
Spacegroup: P3112
Unit cell:
a: 56.71Å b: 56.71Å c: 164.79Å
α: 90° β: 90° γ: 120°
R-values:
R R work R free
0.24 0.239 0.266
Expression system: Escherichia coli