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Crystal structure of mouse CNTN3 IG5-FN2 domains

Analyse Crystal structure of mouse CNTN3 IG5-FN2 domains in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB
5I99
Type
protein
Length
398 residues
Chains
1
Method
x-ray diffraction
Collection
MolNFT v1 / PDB
Contract
0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner
0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule
Contactin-3
UniProt
Q07409
Pockets
2 · best druggability 0.32

Structure

x-ray diffraction · 1 distinct chain · 3% helix, 48% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
AContactin-3protein3983% helix, 48% strandQ07409

Ligands and binding sites

  • GOL · Glycerol · additive · chains A

Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.

Pockets

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

PocketVolume (ų)DruggabilityBuriednessLining residuesInside
1710.320.7517empty
2540.320.7613empty

Modifications

Observed in the structure: 2 disulfide (disulfide).

Compared structures

  • 5I99 · Crystal structure of mouse CNTN3 Ig5-Fn2 domains · the same entry in another collection · chain A against A, TM-score 1.00
  • Q07409 · AlphaFold monomer V2.0 prediction for contactin-3 (Q07409) · a predicted model of the same protein · chain A against A, TM-score 0.58

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