Human phosphomannomutase 2 (PMM2) with mutation T237M in complex with the activator glucose 1,6-bisphosphate

Structure

x-ray diffraction · 1 distinct chain · 41% helix, 20% strand (DSSP).

Ligands and binding sites

• G16 · 1,6-di-O-phosphono-alpha-D-glucopyranose · ligand · chains A
• MG · Magnesium ion · metal · 4 copies · chains A, B
• NA · Sodium ion · metal · 3 copies · chains A, B
• CL · Chloride ion · ion · chains A, B
• GOL · Glycerol · additive · 9 copies · chains A, B

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.

Interfaces

1 interface between chains.

• A–B · 952 Ų buried · 20 hydrogen bonds · protein-protein

Compared structures

• 7O58 · Human phosphomannomutase 2 (PMM2) with mutation T237M in complex with the activator… · the same entry in another collection · chain A against A, TM-score 1.00
• O15305 · AlphaFold monomer V2.0 prediction for phosphomannomutase 2 (O15305) · a predicted model of the same protein · chain A against A, TM-score 0.95

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 O15305
• Elsewhere: RCSB PDB 7O58 · PDBe 7O58 · UniProt O15305