The structure of aplyronine a-actin complex

Structure

x-ray diffraction · 1 distinct chain · 46% helix, 21% strand (DSSP).

Ligands and binding sites

• ATP · Adenosine-5'-triphosphate · ligand · chains A
• AP8 · (8R,9R,10R,11R,14S,18S,20S,24S)-24-{(1R,2S,3R,6R,7R,8R,9S,10E)-8-(acetyloxy)-6-[(N,N-dimethylalanyl)oxy]-11-[formyl(met hyl)amino]-2-hydroxy-1,3,7,9-tetramethylundec-10-enyl}-10-hydroxy-14,20-dimethoxy-9,11,15,18-tetramethyl-2-oxooxacyclote tracosa-3,5,15,21-tetraen-8-yl N,N,O-trimethylserinate · ligand · chains A
• CA · Calcium ion · metal · chains A

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

Pockets

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

Modifications

Observed in the structure: 1 modified (methylation).

Compared structures

• 1WUA · The structure of Aplyronine A-actin complex · the same entry in another collection · chain A against A, TM-score 1.00
• P68135 · AlphaFold monomer V2.0 prediction for actin, alpha skeletal muscle (P68135) · a predicted model of the same protein · chain A against A, TM-score 0.98

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 P68135
• Elsewhere: RCSB PDB 1WUA · PDBe 1WUA · UniProt P68135