2VOG: Mouse A1

Structure of mouse A1 bound to the Bmf BH3-domain. Determined by X-ray diffraction at 1.9 Å resolution. Released 4 Mar 2008.

Method: X-ray diffraction
Resolution: 1.9 Å
Organism: MUS MUSCULUS
Chains: 2
Atoms: 1,394
Mol. weight: 21.27 kDa
Released: 4 Mar 2008

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

Secondary structure: helices and β-sheets

2VOG contains 11 α-helices and 0 β-strands across 2 chains. 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: 10 helices, 0 β-strands

Element	Residues	Length
α-helix	0-20	21
α-helix	32-51	20
α-helix	53-56	4
α-helix	64-78	15
α-helix	79-81	3
α-helix	86-106	21
α-helix	114-136	23
α-helix	139	1
α-helix	140-144	5
α-helix	145-148	4

Chain B: 1 helix, 0 β-strands

Element	Residues	Length	Sheet
α-helix	130-149	20

Molecules and chains

Molecule	Chains	Type	Length	Organism	UniProt
Bcl-2-related protein A1	A	protein	157	MUS MUSCULUS	Q07440 (AlphaFold model)
Bcl-2-modifying factor	B	protein	27	MUS MUSCULUS	Q91ZE9 (AlphaFold model)

Sequence of entity 1 (A), FASTA

>2VOG_1 BCL-2-RELATED PROTEIN A1 (chains A)
GPLGSMAESELMHIHSLAEHYLQYVLQVPAFESAPSQACRVLQRVAFSVQKEVEKNLKSY
LDDFHVESIDTARIIFNQVMEKEFEDGIINWGRIVTIFAFGGVLLKKLKQEQIALDVSAY
KQVSSFVAEFIMNNTGEWIRQNGGWEDGFIKKFEPKS

Sequence of entity 2 (B), FASTA

>2VOG_2 BCL-2-MODIFYING FACTOR (chains B)
LQHRAEVQIARKLQCIADQFHRLHTQQ

Primary citation

Structural Plasticity Underpins Promiscuous Binding of the Prosurvival Protein A1. Smits, C., Czabotar, P.E., Hinds, M.G. et al. Structure (2008) 16:818. DOI 10.1016/J.STR.2008.02.009 · PubMed

Other PDB entries of the same protein (UniProt Q07440 (AlphaFold model), which also has an AlphaFold model), best resolution first:

2VOF 1.8 Å, Structure of mouse A1 bound to the Puma BH3-domain
2VOH 1.9 Å, Structure of mouse A1 bound to the Bak BH3-domain
2VOI 2.1 Å, Structure of mouse A1 bound to the Bid BH3-domain

Browse structure collections

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