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Crystal structure of the kdel receptor in the peptide bound state

Analyse Crystal structure of the kdel receptor in the peptide bound state in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB
6I6H
Type
protein
Length
213 residues
Chains
2
Method
x-ray diffraction
Collection
MolNFT v1 / PDB
Contract
0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner
0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule
Er lumen protein-retaining receptor 2; Aekdel peptide
UniProt
Q5ZKX9
Pockets
1 · best druggability 0.51

Structure

x-ray diffraction · 2 distinct chains · 75% helix, 0% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
AEr lumen protein-retaining receptor 2protein20777% helix, 0% strandQ5ZKX9
BAekdel peptideprotein60% helix, 0% strand—

Ligands and binding sites

  • OLC · (2R)-2,3-dihydroxypropyl (9Z)-octadec-9-enoate · additive · 11 copies · chains A, B

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

Pockets

1 pocket found on a 1 Å grid, 1 with a druggability of 0.5 or more.

PocketVolume (ų)DruggabilityBuriednessLining residuesInside
1650.510.8614empty

Interfaces

1 interface between chains.

  • A–B · 584 Ų buried · 15 hydrogen bonds · protein-protein

Compared structures

  • 6I6H · Crystal structure of the KDEL receptor in the peptide bound state · the same entry in another collection · chain A against A, TM-score 1.00
  • Q5ZKX9 · AlphaFold monomer V2.0 prediction for er lumen protein-retaining receptor 2 (Q5ZKX9) · a predicted model of the same protein · chain A against A, TM-score 0.99

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