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Cryoem structure of mouse PCDH15-4EC-LHFPL5 complex

Analyse Cryoem structure of mouse PCDH15-4EC-LHFPL5 complex in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB
6C13
Type
protein
Length
1,084 residues
Chains
2
Method
electron microscopy
Collection
MolNFT v1 / PDB
Contract
0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner
0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule
Protocadherin-15
UniProt
Q99PJ1
Ligands
NAG, MAN, BMA
Pockets
10 · best druggability 0.80

Structure

electron microscopy · 1 distinct chain · 10% helix, 34% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
A, BProtocadherin-15protein54210% helix, 34% strandQ99PJ1

Ligands and binding sites

  • NAG · 2-acetamido-2-deoxy-beta-D-glucopyranose · sugar · 12 copies · chains A, B
  • MAN · alpha-D-mannopyranose · sugar · 12 copies · chains A, B
  • BMA · beta-D-mannopyranose · sugar · 6 copies · chains A, B

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

Pockets

10 pockets found on a 1 Å grid, 6 with a druggability of 0.5 or more.

PocketVolume (ų)DruggabilityBuriednessLining residuesInside
110100.800.8183empty
21250.770.9529empty
31320.770.9426empty
4700.720.9622empty
51110.610.8736empty

Interfaces

1 interface between chains.

  • A–B · 2176 Ų buried · 20 hydrogen bonds · protein-protein

Modifications

Observed in the structure: 6 glycan (N-glycosylation).

Compared structures

  • 6C13 · CryoEM structure of mouse PCDH15-4EC-LHFPL5 complex · the same entry in another collection · chain A against A, TM-score 1.00
  • Q99PJ1 · AlphaFold monomer V2.0 prediction for protocadherin-15 (Q99PJ1) · a predicted model of the same protein · chain A against A, TM-score 0.57

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