2IMT: Apoptosis regulator BAK

The X-ray Structure of a Bak Homodimer Reveals an Inhibitory Zinc Binding Site. Determined by X-ray diffraction at 1.49 Å resolution. Released 23 Jan 2007.

Method
X-ray diffraction
Resolution
1.49 Å
Organism
Homo sapiens
Chains
1
Atoms
1,422
Mol. weight
19.24 kDa
Ligands
ZN
Released
23 Jan 2007

Explore 2IMT in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

2IMT contains 11 α-helices and 0 β-strands across 1 chain. Residue ranges use author residue numbering, as in the PDB file, from PDBe. To see them in 3D, choose the Cartoon representation with Secondary structure coloring: helices, sheets and coils get different colors.

Chain A: 11 helices, 0 β-strands

ElementResiduesLengthSheet
α-helix24-5027
α-helix51-533
α-helix55-562
α-helix58-603
α-helix70-8516
α-helix87-9711
α-helix104-11916
α-helix125-14420
α-helix151-16414
α-helix167-1737
α-helix177-1826

Molecules and chains

MoleculeChainsTypeLengthOrganismUniProt
Apoptosis regulator BAKAprotein171Homo sapiensQ16611 (AlphaFold model)
Sequence of entity 1 (A), FASTA
>2IMT_1 Apoptosis regulator BAK (chains A)
EPALPSASEEQVAQDTEEVFRSYVFYRHQQEQEAEGVAAPADPEMVTLPLQPSSTMGQVG
RQLAIIGDDINRRYDSEFQTMLQHLQPTAENAYEYFTKIATSLFESGINWGRVVALLGFG
YRLALHVYQHGLTGFLGQVTRFVVDFMLHHCIARWIAQRGGWVAALNLGNG

Ligands and cofactors

IDNameFormulaCopies
ZNZinc ionZn1

Primary citation

The X-ray structure of a BAK homodimer reveals an inhibitory zinc binding site. Moldoveanu, T., Liu, Q., Tocilj, A. et al. Mol Cell (2006) 24:677-688. DOI 10.1016/j.molcel.2006.10.014 · PubMed

Other PDB entries of the same protein (UniProt Q16611 (AlphaFold model), which also has an AlphaFold model), best resolution first:

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