4atm

X-ray diffraction
1.78Å resolution

Crystal structure of the BAR domain of human Amphiphysin, isoform 1 at 1.8 Angstrom resolution featuring increased order at the N- terminus.

Released:
Source organism: Homo sapiens
Entry authors: Allerston CK, Krojer T, Arrowsmith CH, Weigelt J, Edwards A, Bountra C, von Delft F, Gileadi O

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: 243 amino acids
Theoretical weight: 28.55 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: P49418 (Residues: 1-242; Coverage: 35%)
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
Spacegroup: P3221
Unit cell:
a: 82.39Å b: 82.39Å c: 86.59Å
α: 90° β: 90° γ: 120°
R-values:
R R work R free
0.189 0.187 0.218
Expression system: Escherichia coli BL21(DE3)