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Crystal structure of the kdel receptor bound to hdel peptide at pH 6.0

Analyse Crystal structure of the kdel receptor bound to hdel peptide at pH 6.0 in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 6Y7V
Type: protein
Length: 215 residues
Chains: 2
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Er lumen protein-retaining receptor 2; Glu-his-asp-glu-leu
UniProt: Q5ZKX9
Ligands: CO2

Structure

x-ray diffraction · 2 distinct chains · 74% helix, 0% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Er lumen protein-retaining receptor 2	protein	210	76% helix, 0% strand	Q5ZKX9
B	Glu-his-asp-glu-leu	protein	5	0% helix, 0% strand	—

Ligands and binding sites

CO2 · Carbon dioxide · ion · chains A, B
OLC · (2R)-2,3-dihydroxypropyl (9Z)-octadec-9-enoate · additive · 6 copies · chains A

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

Interfaces

1 interface between chains.

A–B · 567 Å² buried · 12 hydrogen bonds · protein-protein

Compared structures

6Y7V · Crystal structure of the KDEL receptor bound to HDEL peptide at pH 6.0 · 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

Analyse

Open in the research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides and crosslinks on the 3D structure
Every structure of UniProt Q5ZKX9
Elsewhere: RCSB PDB 6Y7V · PDBe 6Y7V · UniProt Q5ZKX9

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