› 2d4c

X-ray diffraction
2.4Å resolution

Crystal structure of the endophilin BAR domain mutant

Released:
DOI: 10.2210/pdb2d4c/pdb
PDB entry 2d4c coloured by chain, front view.
PDB entry 2d4c coloured by chain, side view.
PDB entry 2d4c 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 Chains: A, B, C, D
Molecule details ›
Chains: A, B, C, D
Length: 256 amino acids
Theoretical weight: 29.06 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
UniProt:
  • Canonical: Q99962 (Residues: 1-154, 155-247; Coverage: 70%)
Gene names: CNSA2, SH3D2A, SH3GL2
Sequence domains: BAR domain
Structure domains: Arfaptin homology (AH) domain/BAR domain

Ligands and Environments

1 bound ligand:
Ligand CA 1 x CA
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: SPRING-8 BEAMLINE BL38B1
Spacegroup: P21
Unit cell:
a: 44.344Å b: 212.217Å c: 54.317Å
α: 90° β: 96.97° γ: 90°
R-values:
R R work R free
0.217 0.215 0.27
Expression system: Escherichia coli

Quick links

Citations

50 review citations

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

5 mentions without citation

The state of F-BAR domains as membrane-bound oligomeric platforms.
Snider et al. (2021)
4 more