X-ray crystal structure of protein phosphatase-1 with the marine toxin motuporin bound

Structure

x-ray diffraction · 2 distinct chains · 34% helix, 19% strand (DSSP).

Ligands and binding sites

• ACB · 3-methyl-beta-D-aspartic acid · ligand · chains A, B
• 1ZN · (2S,3S,4E,6E,8S,9S)-3-amino-9-methoxy-2,6,8-trimethyl-10-phenyldeca-4,6-dienoic acid · ligand · chains A, B
• FGA · Gamma-D-glutamic acid · ligand · chains A, B
• MDH · N-methyldehydrobutyrine · ligand · chains A
• MN · Manganese (II) ion · metal · 8 copies · chains A
• BME · Beta-mercaptoethanol · additive · 2 copies · 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 · 89 Ų buried · 0 hydrogen bonds · protein-protein

Modifications

Observed in the structure: 4 covalent (additive adduct, covalent ligand).

Compared structures

• 2BCD · X-ray crystal structure of Protein Phosphatase-1 with the marine toxin motuporin bound · the same entry in another collection · chain B against B, TM-score 1.00
• P36873 · AlphaFold monomer V2.0 prediction for SERINE/THREONINE-protein phosphatase PP1-gamma… · a predicted model of the same protein · chain A against A, TM-score 0.99

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 P36873
• Elsewhere: RCSB PDB 2BCD · PDBe 2BCD · UniProt P36873