› 1me8

X-ray diffraction
1.9Å resolution

Inosine Monophosphate Dehydrogenase (IMPDH) From Tritrichomonas Foetus with RVP bound

Released:
DOI: 10.2210/pdb1me8/pdb
PDB entry 1me8 coloured by chain, front view.
PDB entry 1me8 coloured by chain, side view.
PDB entry 1me8 coloured by chain, top view.
Source organism: Tritrichomonas suis
Primary publication:
Crystal structure of Tritrichomonas foetus inosine monophosphate dehydrogenase in complex with the inhibitor ribavirin monophosphate reveals a catalysis-dependent ion-binding site.
Prosise GL, Wu JZ, Luecke H
J Biol Chem 277 50654-9 (2002)
PMID: 12235158

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: 55.56 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

3 bound ligands:
Ligand K 1 x K
Ligand NA 1 x NA
Ligand RVP 1 x RVP
1 modified residue:
Ligand CSO 1 x CSO

Experiments and Validation Details

Entry percentile scores
X-ray source: SSRL BEAMLINE BL9-1
Spacegroup: P432
Unit cell:
a: 154.745Å b: 154.745Å c: 154.745Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.243 0.243 0.258
Expression system: Escherichia coli

Quick links

Citations

3 review citations

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

7 mentions without citation

Chemical approaches to detect and analyze protein sulfenic acids.
Furdui et al. (2014)
6 more