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Crystal structure of beta-catenin and htcf-4

Analyse Crystal structure of beta-catenin and htcf-4 in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 1JDH
Type: protein
Length: 546 residues
Chains: 2
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Beta-catenin; Htcf-4
UniProt: P35222, Q9NQB0
Pockets: 2 · best druggability 0.54

Structure

x-ray diffraction · 2 distinct chains · 74% helix, 0% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Beta-catenin	protein	508	75% helix, 0% strand	P35222
B	Htcf-4	protein	38	55% helix, 0% strand	Q9NQB0

Pockets

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

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	69	0.54	0.87	16	empty
2	76	0.41	0.79	17	empty

Interfaces

1 interface between chains.

A–B · 1797 Å² buried · 28 hydrogen bonds · protein-protein

Compared structures

1JDH · Crystal structure of beta-catenin and htcf-4 · 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 0.97
Q9NQB0 · AlphaFold monomer V2.0 prediction for transcription factor 7-like 2 (Q9NQB0) · a predicted model of the same protein · chain B against A, TM-score 0.35

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 Q9NQB0
Elsewhere: RCSB PDB 1JDH · PDBe 1JDH · UniProt P35222 · UniProt Q9NQB0

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