› 7mtu

X-ray diffraction
2.34Å resolution

Crystal Structure of the Catalytic Domain of the Inosine Monophosphate Dehydrogenase from Bacillus anthracis in the complex with IMP and the inhibitor P221

Released:
DOI: 10.2210/pdb7mtu/pdb
Model geometry
Fit model/data
PDB entry 7mtu coloured by chain, front view.
PDB entry 7mtu coloured by chain, side view.
PDB entry 7mtu coloured by chain, top view.
Source organism: Bacillus anthracis
Entry authors: Kim Y, Maltseva N, Makowska-Grzyska M, Gu M, Gollapalli D, Hedstrom L, Anderson WF, Joachimiak A, Center for Structural Genomics of Infectious Diseases (CSGID)

Function and Biology Details

Reaction catalysed: 
IMP + NAD(+) + H2O = XMP + NADH + H(+).
Biochemical function:
Biological process:
Cellular component:
  • not assigned
Sequence domains:

Structure analysis Details

Assembly composition:
homo tetramer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-105723 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Inosine-5'-monophosphate dehydrogenase Chains: A, B, C, D, E, F, G, H
Molecule details ›
Chains: A, B, C, D, E, F, G, H
Length: 384 amino acids
Theoretical weight: 40.71 KDa
Source organism: Bacillus anthracis
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: A0A6L8P2U9 (Residues: 1-91, 221-487; Coverage: 74%)
Gene names: GBAA_0008, guaB
Sequence domains: IMP dehydrogenase / GMP reductase domain

Ligands and Environments

5 bound ligands:
Ligand IMP 8 x IMP
Ligand GOL 6 x GOL
Ligand ZO7 8 x ZO7
Ligand K 9 x K
Ligand EDO 1 x EDO
No modified residues

Experiments and Validation Details

wwPDB Validation report is not available for this entry.
X-ray source: APS BEAMLINE 19-ID
Spacegroup: P1
Unit cell:
a: 83.27Å b: 89.334Å c: 104.334Å
α: 98.891° β: 90.402° γ: 96.011°
R-values:
R R work R free
0.233 0.231 0.274
Expression system: Escherichia coli BL21(DE3)

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