1DOW: Chimera of beta-catenin and alpha-catenin

Crystal structure of a chimera of beta-catenin and alpha-catenin. Determined by X-ray diffraction at 1.8 Å resolution. Released 12 Jul 2000.

Method: X-ray diffraction
Resolution: 1.8 Å
Organism: Mus musculus
Chains: 2
Atoms: 2,096
Mol. weight: 26.36 kDa
Released: 12 Jul 2000

Explore 1DOW in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

1DOW contains 7 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: 6 helices, 0 β-strands

Element	Residues	Length
α-helix	59-82	24
α-helix	87-113	27
α-helix	118-165	48
α-helix	170-195	26
α-helix	201-230	30
α-helix	235-259	25

Chain B: 1 helix, 0 β-strands

Element	Residues	Length	Sheet
α-helix	121-141	21

Molecules and chains

Molecule	Chains	Type	Length	Organism	UniProt
Alpha-catenin	A	protein	205	Mus musculus	P26231 (AlphaFold model)
Beta-catenin	B	protein	32	Mus musculus	Q02248 (AlphaFold model)

Sequence of entity 1 (A), FASTA

>1DOW_1 ALPHA-CATENIN (chains A)
KAHVLAASVEQATENFLEKGDKIAKESQFLKEELVVAVEDVRKQGDLMKSAAGEFADDPC
SSVKRGNMVRAARALLSAVTRLLILADMADVYKLLVQLKVVEDGILKLRNAGNEQDLGIQ
YKALKPEVDKLNIMAAKRQQELKDVGNRDQMAAARGILQKNVPILYTASQACLQHPDVAA
YKANRDLIYKQLQQAVTGISNAAQA

Sequence of entity 2 (B), FASTA

>1DOW_2 BETA-CATENIN (chains B)
HPTNVQRLAEPSQMLKHAVVNLINYQDDAELA

Primary citation

Structure of the dimerization and beta-catenin-binding region of alpha-catenin. Pokutta, S., Weis, W.I. Mol Cell (2000) 5:533-543. DOI 10.1016/S1097-2765(00)80447-5 · PubMed

Other PDB entries of the same protein (UniProt P26231 (AlphaFold model), which also has an AlphaFold model), best resolution first:

6DV1 2.2 Å, Crystal structure of the alpha-E-catenin actin-binding domain
4E17 2.3 Å, Alpha-E-catenin is an autoinhibited molecule that co-activates vinculin
4E18 2.4 Å, Alpha-E-catenin is an autoinhibited molecule that co-activates vinculin
1L7C 2.5 Å, alpha-catenin fragment, residues 385-651
5Y04 2.85 Å, Crystal Structure of the complex between the vinculin D1 domain and alphaE-catenin
1DOV 3.0 Å, Crystal structure of the alpha-catenin dimerization domain
9DVA 3.1 Å, F-actin binding interface of alpha-E-catenin ABD (cadherin-catenin complex) and afadin
6WVT 3.56 Å, Structural basis of alphaE-catenin - F-actin catch bond behavior
6O3E 4.0 Å, mouse aE-catenin 82-883
4K1N 6.5 Å, Crystal structure of full-length mouse alphaE-catenin

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