› 1mew

X-ray diffraction
2.15Å resolution

Inosine Monophosphate Dehydrogenase (IMPDH) From Tritrichomonas Foetus with XMP and NAD bound

Released:
DOI: 10.2210/pdb1mew/pdb
PDB entry 1mew coloured by chain, front view.
PDB entry 1mew coloured by chain, side view.
PDB entry 1mew coloured by chain, top view.
Source organism: Tritrichomonas suis
Primary publication:
Crystal structures of Tritrichomonasfoetus inosine monophosphate dehydrogenase in complex with substrate, cofactor and analogs: a structural basis for the random-in ordered-out kinetic mechanism.
Prosise GL, Luecke H
J Mol Biol 326 517-27 (2003)
PMID: 12559919

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 domain:

Structure analysis Details

Assembly composition:
homo tetramer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-156124 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Inosine-5'-monophosphate dehydrogenase Chain: A
Molecule details ›
Chain: A
Length: 503 amino acids
Theoretical weight: 55.54 KDa
Source organism: Tritrichomonas suis
Expression system: Escherichia coli
UniProt:
  • Canonical: P50097 (Residues: 1-503; Coverage: 100%)
Gene name: IMPDH
Sequence domains:
Structure domains: Aldolase class I

Ligands and Environments


Cofactor: Ligand NAD 1 x NAD
2 bound ligands:
Ligand K 1 x K
Ligand XMP 1 x XMP
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: ALS BEAMLINE 5.0.2
Spacegroup: P432
Unit cell:
a: 153.827Å b: 153.827Å c: 153.827Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.224 0.224 0.246
Expression system: Escherichia coli

Quick links

Citations

5 review citations

IMP dehydrogenase: structure, mechanism, and inhibition.
Hedstrom L. (2009)
4 more

6 mentions without citation

Compstatin: a complement inhibitor on its way to clinical application.
Ricklin et al. (2008)
5 more