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Crystal structure of alpha-COP/E19 complex

Analyse Crystal structure of alpha-COP/E19 complex in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB
4J8G
Type
protein
Length
620 residues
Chains
4
Method
x-ray diffraction
Collection
MolNFT v1 / PDB
Contract
0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner
0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule
Coatomer subunit alpha; Membrane glycoprotein E3 GP19K
UniProt
Q96WV5
Pockets
3 · best druggability 0.86

Structure

x-ray diffraction · 4 distinct chains · 3% helix, 55% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
ACoatomer subunit alphaprotein2980% helix, 58% strandQ96WV5
BCoatomer subunit alphaprotein3021% helix, 57% strandQ96WV5
CMembrane glycoprotein E3 GP19Kprotein1164% helix, 0% strand—
DMembrane glycoprotein E3 GP19Kprotein967% helix, 0% strand—

Pockets

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

PocketVolume (ų)DruggabilityBuriednessLining residuesInside
19700.860.8774empty
27220.830.8755empty
31500.460.7730empty

Interfaces

4 interfaces between chains.

  • A–B · 474 Ų buried · 4 hydrogen bonds · protein-protein
  • B–C · 437 Ų buried · 16 hydrogen bonds · protein-protein
  • A–D · 411 Ų buried · 14 hydrogen bonds · protein-protein
  • B–D · 228 Ų buried · 0 hydrogen bonds · protein-protein

Compared structures

  • 4J8G · Crystal structure of alpha-COP/E19 complex · the same entry in another collection · chain A against A, TM-score 1.00
  • Q96WV5 · AlphaFold monomer V2.0 prediction for putative coatomer subunit alpha (Q96WV5) · a predicted model of the same protein · chain A against A, TM-score 0.99

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