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Crystal structure of the alpha-N-catenin actin-binding domain H1 mutant

Analyse Crystal structure of the alpha-N-catenin actin-binding domain H1 mutant in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 6DUW
Type: protein
Length: 192 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Catenin alpha-2
UniProt: P26232
Pockets: 1 · best druggability 0.34

Structure

x-ray diffraction · 1 distinct chain · 69% helix, 7% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Catenin alpha-2	protein	192	69% helix, 7% strand	P26232

Pockets

1 pocket found on a 1 Å grid, 0 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	81	0.34	0.74	14	empty

Compared structures

6DUW · Crystal structure of the alpha-N-catenin actin-binding domain H1 mutant · the same entry in another collection · chain A against A, TM-score 1.00
P26232 · AlphaFold monomer V2.0 prediction for catenin alpha-2 (P26232) · a predicted model of the same protein · chain A against A, TM-score 0.93

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 P26232
Elsewhere: RCSB PDB 6DUW · PDBe 6DUW · UniProt P26232

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