Structure of the complex of the extracellular portions of mouse CD200R and mouse CD200

Structure

x-ray diffraction · 2 distinct chains · 2% helix, 58% strand (DSSP).

Ligands and binding sites

• CYS · Cysteine · ligand · chains A
• NAG · 2-acetamido-2-deoxy-beta-D-glucopyranose · sugar · 11 copies · chains A, B
• EDO · 1,2-ethanediol · additive · 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, 0 with a druggability of 0.5 or more.

Interfaces

1 interface between chains.

• A–B · 941 Ų buried · 15 hydrogen bonds · protein-protein

Modifications

Observed in the structure: 11 glycan, 7 disulfide, 1 covalent (N-glycosylation, disulfide, covalent ligand).

Compared structures

• 4BFI · Structure of the complex of the extracellular portions of mouse CD200R and mouse CD200 · the same entry in another collection · chain A against A, TM-score 1.00
• O54901 · AlphaFold monomer V2.0 prediction for ox-2 membrane glycoprotein (O54901) · a predicted model of the same protein · chain B against A, TM-score 0.93
• Q9ES57 · AlphaFold monomer V2.0 prediction for cell surface glycoprotein CD200 receptor 1 (Q9ES57) · a predicted model of the same protein · chain A against A, TM-score 0.90

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 Q9ES57
• Every structure of UniProt O54901
• Elsewhere: RCSB PDB 4BFI · PDBe 4BFI · UniProt Q9ES57 · UniProt O54901