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The crystal structure of BAK1 - a mitochondrial apoptosis regulator

Analyse The crystal structure of BAK1 - a mitochondrial apoptosis regulator in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB
2JCN
Type
protein
Length
157 residues
Chains
1
Method
x-ray diffraction
Collection
MolNFT v1 / PDB
Contract
0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner
0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule
BCL-2 homologous ANTAGONIST/KILLER
UniProt
Q16611
Ligands
SO4

Structure

x-ray diffraction · 1 distinct chain · 75% helix, 0% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
ABCL-2 homologous ANTAGONIST/KILLERprotein15775% helix, 0% strandQ16611

Ligands and binding sites

  • SO4 · Sulfate ion · ion · chains A

Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.

Compared structures

  • 2JCN · The crystal structure of BAK1 - a mitochondrial apoptosis regulator · the same entry in another collection · chain A against A, TM-score 1.00
  • Q16611 · AlphaFold monomer V2.0 prediction for BCL-2 homologous ANTAGONIST/KILLER (Q16611) · a predicted model of the same protein · chain A against A, TM-score 0.94

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