Research workbench

Beta-catenin in complex with a phosphorylated apc 20AA repeat fragment

Analyse Beta-catenin in complex with a phosphorylated apc 20AA repeat fragment in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 1TH1
Type: protein
Length: 1,137 residues
Chains: 4
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Beta-catenin; Adenomatous polyposis COLI protein
UniProt: P35222, P25054
Pockets: 11 · best druggability 0.65

Structure

x-ray diffraction · 4 distinct chains · 69% helix, 1% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Beta-catenin	protein	514	73% helix, 1% strand	P35222
B	Beta-catenin	protein	513	74% helix, 0% strand	P35222
C	Adenomatous polyposis COLI protein	protein	56	27% helix, 0% strand	P25054
D	Adenomatous polyposis COLI protein	protein	54	28% helix, 0% strand	P25054

Pockets

11 pockets found on a 1 Å grid, 4 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	367	0.65	0.80	40	empty
2	389	0.64	0.78	44	empty
3	249	0.62	0.81	38	empty
4	188	0.61	0.83	25	empty
5	153	0.48	0.78	31	empty

Interfaces

3 interfaces between chains.

A–C · 2649 Å² buried · 38 hydrogen bonds · protein-protein
B–D · 2616 Å² buried · 44 hydrogen bonds · protein-protein
A–B · 954 Å² buried · 5 hydrogen bonds · protein-protein

Modifications

Observed in the structure: 10 modified (phosphorylation).

Compared structures

1TH1 · Beta-catenin in complex with a phosphorylated APC 20aa repeat fragment · the same entry in another collection · chain A against A, TM-score 1.00
P35222 · AlphaFold monomer V2.0 prediction for catenin beta-1 (P35222) · a predicted model of the same protein · chain A against A, TM-score 0.99

Analyse

Open in the research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides and crosslinks on the 3D structure
Every structure of UniProt P35222
Every structure of UniProt P25054
Elsewhere: RCSB PDB 1TH1 · PDBe 1TH1 · UniProt P35222 · UniProt P25054

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