2jcn

X-ray diffraction
1.8Å resolution

The crystal structure of BAK1 - a mitochondrial apoptosis regulator

Released:
Source organism: Homo sapiens
Entry authors: Moche M, Stenmark P, Arrowsmith C, Berglund H, Busam R, Collins R, Edwards A, Ericsson UB, Flodin S, Flores A, Graslund S, Hammarstrom M, Hallberg BM, Holmberg Schiavone L, Johansson I, Karlberg T, Kosinska U, Kotenyova T, Lundgren S, Nilsson ME, Nyman T, Ogg D, Persson C, Sagemark J, Sundstrom M, Uppenberg J, Upsten M, Thorsell AG, van den Berg S, Weigelt J, Nordlund P, Structural Genomics Consortium (SGC)

Function and Biology Details

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

Structure analysis Details

Assembly composition:
monomeric (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Bcl-2 homologous antagonist/killer Chain: A
Molecule details ›
Chain: A
Length: 172 amino acids
Theoretical weight: 19.32 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: Q16611 (Residues: 21-190; Coverage: 81%)
Gene names: BAK, BAK1, BCL2L7, CDN1
Sequence domains: Apoptosis regulator proteins, Bcl-2 family
Structure domains: Blc2-like

Ligands and Environments

1 bound ligand:
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: ESRF BEAMLINE ID14-2
Spacegroup: P6522
Unit cell:
a: 62.77Å b: 62.77Å c: 138.07Å
α: 90° β: 90° γ: 120°
R-values:
R R work R free
0.189 0.187 0.232
Expression system: Escherichia coli BL21(DE3)