The structure of human MAT2A in complex with S-adenosylethionine and ppnp.

Structure

x-ray diffraction · 1 distinct chain · 33% helix, 26% strand (DSSP).

Ligands and binding sites

• PPK · (diphosphono)aminophosphonic acid · ligand · chains A
• S7M · [(3S)-3-amino-3-carboxypropyl]{[(2S,3S,4R,5R)-5-(6-amino-9H-purin-9-yl)-3,4-dihydroxytetrahydrofuran-2-yl]methyl}ethyls ulfonium · ligand · chains A
• MG · Magnesium ion · metal · 2 copies · chains A
• K · Potassium ion · metal · chains A
• MPD · (4S)-2-methyl-2,4-pentanediol · additive · 2 copies · chains A
• IMD · Imidazole · additive · 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, 0 with a druggability of 0.5 or more.

Compared structures

• 5A1G · The structure of Human MAT2A in complex with S-adenosylethionine and PPNP. · the same entry in another collection · chain A against A, TM-score 1.00
• P31153 · AlphaFold monomer V2.0 prediction for S-adenosylmethionine synthase isoform type-2… · 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 P31153
• Elsewhere: RCSB PDB 5A1G · PDBe 5A1G · UniProt P31153