› 6uaj

Electron Microscopy
3.84Å resolution

Human IMPDH2 treated with ATP, IMP, NAD+, and 2 mM GTP. Free canonical octamer reconstruction.

Released:
DOI: 10.2210/pdb6uaj/pdb
PDB entry 6uaj coloured by chain, front view.
PDB entry 6uaj coloured by chain, side view.
PDB entry 6uaj coloured by chain, top view.
Source organism: Homo sapiens
Primary publication:
Cryo-EM structures demonstrate human IMPDH2 filament assembly tunes allosteric regulation.
Johnson MC, Kollman JM
OpenAccess logo Elife 9 (2020)
PMID: 31999252
Related structures: EMD-20706, EMD-20688, EMD-20707, EMD-20690, EMD-20691, EMD-20704, EMD-20701, EMD-20687, EMD-20705

Function and Biology Details

Reaction catalysed: 
Inosine 5'-phosphate + NAD(+) + H(2)O = xanthosine 5'-phosphate + NADH
Biochemical function:
Biological process:
Cellular component:
Sequence domains:

Structure analysis Details

Assembly composition:
homo octamer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-146110 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Inosine-5'-monophosphate dehydrogenase 2 Chains: A, B, C, D, E, F, G, H
Molecule details ›
Chains: A, B, C, D, E, F, G, H
Length: 519 amino acids
Theoretical weight: 56.48 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
UniProt:
  • Canonical: P12268 (Residues: 1-514; Coverage: 100%)
Gene names: IMPD2, IMPDH2
Sequence domains:

Ligands and Environments


Cofactor: Ligand NAD 8 x NAD
3 bound ligands:
Ligand GTP 16 x GTP
Ligand ATP 8 x ATP
Ligand IMP 8 x IMP
No modified residues

Experiments and Validation Details

Entry percentile scores
Resolution: 3.84Å
Relevant EMDB volumes: EMD-20687, EMD-20688, EMD-20690, EMD-20691, EMD-20701, EMD-20704, EMD-20705, EMD-20706, EMD-20707
Expression system: Escherichia coli

Quick links

Citations

6 review citations

Targeting cancer metabolism in the era of precision oncology.
Stine et al. (2022)
5 more