Human IMPDH2 treated with ATP, imp, NAD+, and 2 mm GTP. free canonical octamer reconstruction.

Structure

electron microscopy · 1 distinct chain · 29% helix, 16% strand (DSSP).

Ligands and binding sites

• GTP · Guanosine-5'-triphosphate · ligand · 16 copies · chains A, B, C, D, E, F, G, H
• ATP · Adenosine-5'-triphosphate · ligand · 8 copies · chains A, F, B, E, C, H, D, G
• IMP · Inosinic acid · ligand · 8 copies · chains A, B, C, D, E, F, G, H
• NAD · Nicotinamide-adenine-dinucleotide · ligand · 8 copies · chains A, D, B, C, E, H, F, G

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

Pockets

20 pockets found on a 1 Å grid, 20 with a druggability of 0.5 or more.

Interfaces

20 interfaces between chains.

• E–H · 2316 Ų buried · 32 hydrogen bonds · protein-protein
• F–G · 2316 Ų buried · 30 hydrogen bonds · protein-protein
• B–C · 2310 Ų buried · 30 hydrogen bonds · protein-protein
• A–D · 2302 Ų buried · 29 hydrogen bonds · protein-protein
• A–B · 2300 Ų buried · 31 hydrogen bonds · protein-protein

Modifications

Observed in the structure: 16 covalent (covalent ligand).

Compared structures

• 6UAJ · Human IMPDH2 treated with ATP, IMP, NAD+, and 2 mM GTP. Free canonical octamer… · the same entry in another collection · chain H against H, TM-score 1.00
• P12268 · AlphaFold monomer V2.0 prediction for inosine-5'-monophosphate dehydrogenase 2 (P12268) · 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 P12268
• Elsewhere: RCSB PDB 6UAJ · PDBe 6UAJ · UniProt P12268