1T08: Beta-catenin

Crystal structure of beta-catenin/ICAT helical domain/unphosphorylated APC R3. Determined by X-ray diffraction at 2.1 Å resolution. Released 12 Oct 2004.

Method: X-ray diffraction
Resolution: 2.1 Å
Organism: Homo sapiens
Chains: 3
Atoms: 4,697
Mol. weight: 63.46 kDa
Released: 12 Oct 2004

Explore 1T08 in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

1T08 contains 42 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: 38 helices, 0 β-strands

Element	Residues	Length
α-helix	147	1
α-helix	148-152	5
α-helix	153-159	7
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	236-242	7
α-helix	243-245	3
α-helix	249-265	17
α-helix	269-275	7
α-helix	278-285	8
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
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	649-663	15

Chain B: 4 helices, 0 β-strands

Element	Residues	Length
α-helix	11-28	18
α-helix	31-34	4
α-helix	35-43	9
α-helix	45-52	8

Molecules and chains

Molecule	Chains	Type	Length	Organism	UniProt
Beta-catenin	A	protein	519	Homo sapiens	P35222 (AlphaFold model)
Beta-catenin-interacting protein 1	B	protein	46	Homo sapiens	Q9NSA3 (AlphaFold model)
Adenomatous polyposis coli protein	C	protein	15	Homo sapiens	P25054

Sequence of entity 1 (A), FASTA

>1T08_1 Beta-catenin (chains A)
AELATRAIPELTKLLNDEDQVVVNKAAVMVHQLSKKEASRHAIMRSPQMVSAIVRTMQNT
NDVETARCTAGTLHNLSHHREGLLAIFKSGGIPALVKMLGSPVDSVLFYAITTLHNLLLH
QEGAKMAVRLAGGLQKMVALLNKTNVKFLAITTDCLQILAYGNQESKLIILASGGPQALV
NIMRTYTYEKLLWTTSRVLKVLSVCSSNKPAIVEAGGMQALGLHLTDPSQRLVQNCLWTL
RNLSDAATKQEGMEGLLGTLVQLLGSDDINVVTCAAGILSNLTCNNYKNKMMVCQVGGIE
ALVRTVLRAGDREDITEPAICALRHLTSRHQEAEMAQNAVRLHYGLPVVVKLLHPPSHWP
LIKATVGLIRNLALCPANHAPLREQGAIPRLVQLLVRAHQDTQRRTSMGGTQQQFVEGVR
MEEIVEGCTGALHILARDVHNRIVIRGLNTIPLFVQLLYSPIENIQRVAAGVLCELAQDK
EAAEAIEAEGATAPLTELLHSRNEGVATYAAAVLFRMSE

Sequence of entity 2 (B), FASTA

>1T08_2 Beta-catenin-interacting protein 1 (chains B)
GKSPEEMYIQQKVRVLLMLRKMGSNLTASEEEFLRTYAGVVNSQLS

Sequence of entity 3 (C), FASTA

>1T08_3 Adenomatous polyposis coli protein (chains C)
DADTLLHFATESTPD

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) 15:511-521. DOI 10.1016/j.molcel.2004.08.010 · PubMed

Other PDB entries of the same protein (UniProt P35222 (AlphaFold model), which also has an AlphaFold model), best resolution first:

3FQN 1.65 Å, Phosphorylation of self-peptides alters Human Leukocyte Antigen Class I-restricted…
3FQR 1.7 Å, Phosphorylation of self-peptides alters Human Leukocyte Antigen Class I-restricted…
7AFW 1.81 Å, Beta-Catenin in complex with compound 6
1JDH 1.9 Å, Crystal structure of beta-catenin and htcf-4
9I8K 2.0 Å, Beta-catenin armadillo (150-663)
9I8X 2.0 Å, Beta-catenin armadillo with cyclic peptide and Compound 2
8RU3 2.0 Å, Crystal structure of beta-catenin in complex with alpha-helical peptide inhibitor
6M90 2.05 Å, Monophosphorylated pSer33 b-Catenin peptide, b-TrCP/Skp1, NRX-2776 ternary complex
29KL 2.09 Å, Crystal structure of Human Catenin Beta-1 in complex with cyclic beta sheet peptide…
1G3J 2.1 Å, Crystal structure of the XTCF3-cbd/beta-catenin armadillo repeat complex
3DIW 2.1 Å, c-terminal beta-catenin bound TIP-1 structure
8RU4 2.13 Å, Crystal structure of Human Catenin Beta-1 in complex with stitched peptide inhibitor

Browse structure collections

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