› 4ddp

X-ray diffraction
1.55Å resolution

crystal structure of Beclin 1 evolutionarily conserved domain(ECD)

Released:
DOI: 10.2210/pdb4ddp/pdb
PDB entry 4ddp coloured by chain, front view.
PDB entry 4ddp coloured by chain, side view.
PDB entry 4ddp coloured by chain, top view.
Source organism: Homo sapiens
Primary publication:
Crystal structure and biochemical analyses reveal Beclin 1 as a novel membrane binding protein.
Huang W, Choi W, Hu W, Mi N, Guo Q, Ma M, Liu M, Tian Y, Lu P, Wang FL, Deng H, Liu L, Gao N, Yu L, Shi Y
Cell Res 22 473-89 (2012)
PMID: 22310240

Function and Biology Details

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

Structure analysis Details

Assembly composition:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-172007 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Beclin-1-C 35 kDa Chain: A
Molecule details ›
Chain: A
Length: 210 amino acids
Theoretical weight: 24.46 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
UniProt:
  • Canonical: Q14457 (Residues: 241-450; Coverage: 47%)
Gene names: BECN1, GT197
Sequence domains: Apg6 BARA domain
Structure domains: Autophagy protein 6/Beclin 1

Ligands and Environments

No bound ligands
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: SPRING-8 BEAMLINE BL41XU
Spacegroup: C2
Unit cell:
a: 80.746Å b: 33.563Å c: 74.765Å
α: 90° β: 113.49° γ: 90°
R-values:
R R work R free
0.177 0.176 0.203
Expression system: Escherichia coli

Quick links

Citations

48 review citations

Autophagy in infection, inflammation and immunity.
Deretic et al. (2013)
47 more

23 mentions without citation

Conformational flexibility of BECN1: Essential to its key role in autophagy and beyond.
Mei et al. (2016)
22 more