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Protocadherin gamma B2 extracellular cadherin domains 1-5

Analyse Protocadherin gamma B2 extracellular cadherin domains 1-5 in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB
5T9T
Type
protein
Length
1,052 residues
Chains
2
Method
x-ray diffraction
Collection
MolNFT v1 / PDB
Contract
0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner
0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule
Protocadherin gamma B2-alpha C
UniProt
Q8K486
Ligands
MAN, NAG, BMA, FUC, CA
Pockets
7 · best druggability 0.58

Structure

x-ray diffraction · 2 distinct chains · 6% helix, 45% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
AProtocadherin gamma B2-alpha Cprotein5267% helix, 46% strandQ8K486
BProtocadherin gamma B2-alpha Cprotein5266% helix, 45% strandQ8K486

Ligands and binding sites

  • MAN · alpha-D-mannopyranose · sugar · 11 copies · chains A, B
  • NAG · 2-acetamido-2-deoxy-beta-D-glucopyranose · sugar · 5 copies · chains B, A
  • BMA · beta-D-mannopyranose · sugar
  • FUC · alpha-L-fucopyranose · sugar · chains B
  • CA · Calcium ion · metal · 26 copies · chains A, B

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

Pockets

7 pockets found on a 1 Å grid, 4 with a druggability of 0.5 or more.

PocketVolume (ų)DruggabilityBuriednessLining residuesInside
12860.580.7836empty
21320.540.8225empty
31160.520.8123empty
41870.510.7734empty
51320.420.7617empty

Interfaces

1 interface between chains.

  • A–B · 2148 Ų buried · 23 hydrogen bonds · protein-protein

Modifications

Observed in the structure: 15 glycan, 2 disulfide (O-glycosylation, N-glycosylation, disulfide).

Compared structures

  • 5T9T · Protocadherin Gamma B2 extracellular cadherin domains 1-5 · the same entry in another collection · chain A against A, TM-score 1.00

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