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Crystal structure of zebrafish protocadherin-19 EC3-4

Analyse Crystal structure of zebrafish protocadherin-19 EC3-4 in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB
5CO1
Type
protein
Length
831 residues
Chains
4
Method
x-ray diffraction
Collection
MolNFT v1 / PDB
Contract
0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner
0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule
Protocadherin-19 isoform 1
UniProt
C4P340
Ligands
CA
Pockets
5 · best druggability 0.73

Structure

x-ray diffraction · 3 distinct chains · 4% helix, 48% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
AProtocadherin-19 isoform 1protein2063% helix, 48% strandC4P340
BProtocadherin-19 isoform 1protein2054% helix, 50% strandC4P340
C, DProtocadherin-19 isoform 1protein2105% helix, 47% strandC4P340

Ligands and binding sites

  • CA · Calcium ion · metal · 16 copies · chains A, B, C, D

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

Pockets

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

PocketVolume (ų)DruggabilityBuriednessLining residuesInside
18560.730.7887empty
23520.640.7934empty
32290.500.7535empty
41770.460.7523empty
51890.460.7528empty

Interfaces

4 interfaces between chains.

  • A–C · 566 Ų buried · 8 hydrogen bonds · protein-protein
  • C–D · 545 Ų buried · 4 hydrogen bonds · protein-protein
  • A–B · 506 Ų buried · 0 hydrogen bonds · protein-protein
  • A–D · 202 Ų buried · 2 hydrogen bonds · protein-protein

Compared structures

  • 5CO1 · Crystal Structure of Zebrafish Protocadherin-19 EC3-4 · the same entry in another collection · chain A against A, TM-score 1.00

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