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Crystal structure of mouse CNTN2 FN1-FN3 domains

Analyse Crystal structure of mouse CNTN2 FN1-FN3 domains in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 5E7L
Type: protein
Length: 302 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Contactin-2
UniProt: Q61330
Pockets: 1 · best druggability 0.44

Structure

x-ray diffraction · 1 distinct chain · 2% helix, 45% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Contactin-2	protein	302	2% helix, 45% strand	Q61330

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	90	0.44	0.79	19	empty

Compared structures

5E7L · Crystal structure of mouse CNTN2 FN1-FN3 domains · the same entry in another collection · chain A against A, TM-score 1.00
Q61330 · AlphaFold monomer V2.0 prediction for contactin-2 (Q61330) · a predicted model of the same protein · chain A against A, TM-score 0.71

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 Q61330
Elsewhere: RCSB PDB 5E7L · PDBe 5E7L · UniProt Q61330

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