AlphaFold monomer V2.0 prediction for wiskott-aldrich syndrome protein (P42768)

Structure

1 distinct chain · 20% helix, 12% strand (DSSP).

Pockets

1 pocket found on a 1 Å grid, 0 with a druggability of 0.5 or more.

Compared structures

• 1EJ5 · Solution structure of the autoinhibited conformation of wasp · an experimental structure of the same protein · chain A against A, TM-score 0.16
• 1EJ5 · Solution structure of the autoinhibited conformation of wasp · an experimental structure of the same protein · chain A against A, TM-score 0.16
• 1T84 · Solution structure of the Wiskott-Aldrich Syndrome Protein (WASP) autoinhibited core… · an experimental structure of the same protein · chain A against A, TM-score 0.16
• 1T84 · Solution structure of the wiskott-aldrich syndrome protein (wasp) autoinhibited core… · an experimental structure of the same protein · chain A against A, TM-score 0.16
• 2K42 · Solution Structure of the GTPase Binding Domain of WASP in Complex with EspFU, an EHEC… · an experimental structure of the same protein · chain A against A, TM-score 0.12
• 2K42 · Solution structure of the GTPase binding domain of wasp in complex with espfu, an ehec… · an experimental structure of the same protein · chain A against A, TM-score 0.12
• 1CEE · Solution structure of CDC42 in complex with the GTPase binding domain of wasp · an experimental structure of the same protein · chain A against B, TM-score 0.08
• 1CEE · Solution structure of CDC42 in complex with the GTPase binding domain of wasp · an experimental structure of the same protein · chain A against B, TM-score 0.08
• 2OT0 · Fructose-1,6-bisphosphate aldolase from rabbit muscle in complex with a C-terminal… · an experimental structure of the same protein · chain A against E, TM-score 0.01
• 2OT0 · Fructose-1,6-bisphosphate aldolase from rabbit muscle in complex with a C-terminal… · an experimental structure of the same protein · chain A against E, TM-score 0.01

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 P42768
• Elsewhere: UniProt P42768 · AlphaFold DB P42768