1V18: Beta-catenin armadillo repeat

The crystal structure of beta-catenin armadillo repeat complexed with a phosphorylated APC 20mer repeat. Determined by X-ray diffraction at 2.1 Å resolution. Released 12 Jan 2005.

Method: X-ray diffraction
Resolution: 2.1 Å
Organisms: MUS MUSCULUS, HOMO SAPIENS
Chains: 2
Atoms: 4,430
Mol. weight: 64.26 kDa
Released: 12 Jan 2005

Explore 1V18 in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

1V18 contains 38 α-helices and 2 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: 36 helices, 2 β-strands

Element	Residues	Length	Sheet
α-helix	152-160	9
α-helix	165-179	15
α-helix	182-189	8
α-helix	192-202	11
α-helix	208-221	14
α-helix	225-233	9
α-helix	236-243	8
α-helix	249-265	17
α-helix	269-275	7
α-helix	278-284	7
α-helix	285-287	3
α-helix	291-305	15
α-helix	309-317	9
α-helix	320-330	11
α-helix	334-347	14
α-helix	353-359	7
α-helix	362-367	6
α-helix	375-389	15
α-helix	399-408	10
α-helix	414-427	14
α-helix	432-440	9
α-helix	443-454	12
α-helix	458-471	14
α-helix	478-487	10
α-helix	491-496	6
α-helix	504-517	14
α-helix	521-523	3
α-helix	524-529	6
α-helix	532-548	17
β-strand	561	1	1
β-strand	564	1	1
α-helix	566-580	15
α-helix	584-592	9
α-helix	596-602	7
α-helix	608-621	14
α-helix	625-633	9
α-helix	637-643	7
α-helix	649-662	14

Chain B: 2 helices, 0 β-strands

Element	Residues	Length	Sheet
α-helix	1505-1509	5
α-helix	1520-1524	5

Molecules and chains

Molecule	Chains	Type	Length	Organism	UniProt
Beta-catenin	A	protein	538	MUS MUSCULUS	Q02248 (AlphaFold model)
Adenomatous polyposis coli	B	protein	47	HOMO SAPIENS	P25054

Sequence of entity 1 (A), FASTA

>1V18_1 BETA-CATENIN (chains A)
HAVVNLINYQDDAELATRAIPELTKLLNDEDQVVVNKAAVMVHQLSKKEASRHAIMRSPQ
MVSAIVRTMQNTNDVETARCTAGTLHNLSHHREGLLAIFKSGGIPALVKMLGSPVDSVLF
YAITTLHNLLLHQEGAKMAVRLAGGLQKMVALLNKTNVKFLAITTDCLQILAYGNQESKL
IILASGGPQALVNIMRTYTYEKLLWTTSRVLKVLSVCSSNKPAIVEAGGMQALGLHLTDP
SQRLVQNCLWTLRNLSDAATKQEGMEGLLGTLVQLLGSDDINVVTCAAGILSNLTCNNYK
NKMMVCQVGGIEALVRTVLRAGDREDITEPAICALRHLTSRHQEAEMAQNAVRLHYGLPV
VVKLLHPPSHWPLIKATVGLIRNLALCPANHAPLREQGAIPRLVQLLVRAHQDTQRRTSM
GGTQQQFVEGVRMEEIVEGCTGALHILARDVHNRIVIRGLNTIPLFVQLLYSPIENIQRV
AAGVLCELAQDKEAAEAIEAEGATAPLTELLHSRNEGVATYAAAVLFRMSEDKPQDYK

Sequence of entity 2 (B), FASTA

>1V18_2 ADENOMATOUS POLYPOSIS COLI (chains B)
LPDADTLLHFATESTPDGFSCSSSLSALSLDEPFIQKDVELRIMPPV

Primary citation

Mechanism of Phosphorylation-Dependent Binding of Apc to Beta-Catenin and its Role in Beta-Catenin Degradation. Ha, N.-C., Tonozuka, T., Stamos, J.L. et al. Mol Cell (2004) 15:511. DOI 10.1016/J.MOLCEL.2004.08.010 · PubMed

Other PDB entries of the same protein (UniProt Q02248 (AlphaFold model), which also has an AlphaFold model), best resolution first:

1DOW 1.8 Å, Crystal structure of a chimera of beta-catenin and alpha-catenin
4EV8 1.9 Å, Crystal structure of mouse catenin beta-59 in 2.4M urea.
1I7W 2.0 Å, Beta-catenin/phosphorylated E-cadherin complex
4EVA 2.0 Å, Crystal Structure of Mouse Catenin beta-59 in 5.6M urea
1M1E 2.1 Å, Beta-catenin armadillo repeat domain bound to ICAT
3BCT 2.1 Å, The armadillo repeat region from murine beta-catenin
4EV9 2.1 Å, Crystal Structure of Mouse Catenin beta-59 in 4.0M urea
4EVP 2.25 Å, Crystal Structure of Mouse Catenin beta-59 in 7.2M urea
4EVT 2.34 Å, Crystal Structure of Mouse Catenin beta-59 in 8.3M urea
3OUX 2.4 Å, Structure of beta-catenin with phosphorylated Lef-1
4ONS 2.8 Å, Structural and thermodynamic characterization of cadherin-beta-catenin-alpha-catenin…
2BCT 2.9 Å, The armadillo repeat region from murine beta-catenin

Browse structure collections

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