AlphaFold monomer V2.0 prediction for gastric inhibitory polypeptide (P09681)

Structure

1 distinct chain.

Compared structures

• 2L70 · NMR solution structure of GIP in micellular media · an experimental structure of the same protein · chain A against A, TM-score 0.21
• 2L70 · NMR solution structure of gip in micellular media · an experimental structure of the same protein · chain A against A, TM-score 0.21
• 2OBU · Solution structure of GIP in TFE/water · an experimental structure of the same protein · chain A against A, TM-score 0.20
• 2OBU · Solution structure of gip in TFE/WATER · an experimental structure of the same protein · chain A against A, TM-score 0.20
• 2B4N · Solution structure of glucose-dependent insulinotropic polypeptide · an experimental structure of the same protein · chain A against A, TM-score 0.19
• 2B4N · Solution Structure of Glucose-Dependent Insulinotropic Polypeptide · an experimental structure of the same protein · chain A against A, TM-score 0.19
• 7DTY · Structural basis of ligand selectivity conferred by the human glucose- dependent… · an experimental structure of the same protein · chain A against P, TM-score 0.19
• 7RA3 · Cryo-EM of human gastric inhibitory polypeptide receptor gipr bound to gip · an experimental structure of the same protein · chain A against P, TM-score 0.19
• 2L71 · NMR solution structure of gip in bicellular media · an experimental structure of the same protein · chain A against A, TM-score 0.19
• 2L71 · NMR solution structure of GIP in Bicellular media · an experimental structure of the same protein · chain A against A, TM-score 0.19
• 2QKH · Crystal structure of the extracellular domain of human GIP receptor in complex with the… · an experimental structure of the same protein · chain A against B, TM-score 0.18
• 2QKH · Crystal structure of the extracellular domain of human gip receptor in complex with the… · an experimental structure of the same protein · chain A against B, TM-score 0.18

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 P09681
• Elsewhere: UniProt P09681 · AlphaFold DB P09681