AlphaFold monomer V2.0 prediction for orexin receptor type 2 (O43614)

Structure

1 distinct chain · 66% helix, 3% strand (DSSP).

Pockets

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

Modifications

Observed in the structure: 1 disulfide (disulfide).

Compared structures

• 5WS3 · Crystal structures of human orexin 2 receptor bound to the selective antagonist empa… · an experimental structure of the same protein · chain A against A, TM-score 0.75
• 5WQC · Crystal structure of human orexin 2 receptor bound to the selective antagonist empa… · an experimental structure of the same protein · chain A against A, TM-score 0.73
• 6TPJ · Crystal structure of the orexin-2 receptor in complex with suvorexant at 2.76 a resolution · an experimental structure of the same protein · chain A against B, TM-score 0.73
• 6TPJ · Crystal structure of the Orexin-2 receptor in complex with suvorexant at 2.76 A resolution · an experimental structure of the same protein · chain A against B, TM-score 0.73
• 6TPN · Crystal structure of the orexin-2 receptor in complex with HTL6641 at 2.61 a resolution · an experimental structure of the same protein · chain A against A, TM-score 0.73
• 6TPG · Crystal structure of the orexin-2 receptor in complex with empa at 2.74 a resolution · an experimental structure of the same protein · chain A against A, TM-score 0.73
• 4S0V · Crystal structure of the human OX2 orexin receptor bound to the insomnia drug Suvorexant · an experimental structure of the same protein · chain A against A, TM-score 0.69
• 4S0V · Crystal structure of the human OX2 orexin receptor bound to the insomnia drug suvorexant · an experimental structure of the same protein · chain A against A, TM-score 0.69
• 7SQO · Structure of the orexin-2 RECEPTOR(OX2R) bound to tak-925, gi and SCFV16 · an experimental structure of the same protein · chain A against R, TM-score 0.57

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 O43614
• Elsewhere: UniProt O43614 · AlphaFold DB O43614