› 1x04

X-ray diffraction
2.9Å resolution

Crystal structure of endophilin BAR domain (mutant)

Released:
DOI: 10.2210/pdb1x04/pdb
PDB entry 1x04 coloured by chain, front view.
PDB entry 1x04 coloured by chain, side view.
PDB entry 1x04 coloured by chain, top view.
Source organism: Homo sapiens
Primary publication:
Endophilin BAR domain drives membrane curvature by two newly identified structure-based mechanisms.
Masuda M, Takeda S, Sone M, Ohki T, Mori H, Kamioka Y, Mochizuki N
EMBO J 25 2889-97 (2006)
PMID: 16763557

Function and Biology Details

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

Structure analysis Details

Assembly composition:
homo dimer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-189292 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Endophilin-A1 Chain: A
Molecule details ›
Chain: A
Length: 230 amino acids
Theoretical weight: 26.61 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
UniProt:
  • Canonical: Q99962 (Residues: 1-58, 89-247; Coverage: 62%)
Gene names: CNSA2, SH3D2A, SH3GL2
Sequence domains: BAR domain
Structure domains: Arfaptin homology (AH) domain/BAR domain

Ligands and Environments

No bound ligands
1 modified residue:
Ligand MSE 8 x MSE

Experiments and Validation Details

Entry percentile scores
X-ray source: SPRING-8 BEAMLINE BL45PX
Spacegroup: I41
Unit cell:
a: 129.077Å b: 129.077Å c: 97.963Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.24 0.238 0.269
Expression system: Escherichia coli

Quick links

Citations

50 review citations

Membrane recognition by phospholipid-binding domains.
Lemmon MA. (2008)
49 more

3 mentions without citation

Endophilin BAR domain drives membrane curvature by two newly identified structure-based mechanisms.
Masuda et al. (2006)
2 more