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Crystal structure of the kdel receptor in the peptide free state.

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

PDB
6I6B
Type
protein
Length
203 residues
Chains
1
Method
x-ray diffraction
Collection
MolNFT v1 / PDB
Contract
0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner
0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule
Er lumen protein-retaining receptor 2
UniProt
Q5ZKX9
Pockets
1 · best druggability 0.71

Structure

x-ray diffraction · 1 distinct chain · 76% helix, 0% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
AEr lumen protein-retaining receptor 2protein20376% helix, 0% strandQ5ZKX9

Ligands and binding sites

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

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
13130.710.8434empty

Compared structures

  • 6I6B · Crystal structure of the KDEL receptor in the peptide free 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 0.94

Analyse

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