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X-ray diffraction
1.6Å resolution

Crystal Structure of the Catalytic Domain of the Inosine Monophosphate Dehydrogenase from Mycobacterium tuberculosis in the complex with XMP and NAD

Released:

Function and Biology Details

Reaction catalysed:
Inosine 5'-phosphate + NAD(+) + H(2)O = xanthosine 5'-phosphate + NADH
Biochemical function:
Cellular component:
  • not assigned

Structure analysis Details

Assembly composition:
homo tetramer (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Inosine-5'-monophosphate dehydrogenase Chain: A
Molecule details ›
Chain: A
Length: 407 amino acids
Theoretical weight: 41.64 KDa
Source organism: Mycobacterium tuberculosis H37Rv
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: P9WKI7 (Residues: 1-125, 253-529; Coverage: 76%)
Gene names: MTCY78.17, Rv3411c, guaB, guaB2
Sequence domains: IMP dehydrogenase / GMP reductase domain
Structure domains: Aldolase class I

Ligands and Environments


Cofactor: Ligand NAD 1 x NAD
1 bound ligand:
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: APS BEAMLINE 19-ID
Spacegroup: I4
Unit cell:
a: 88.154Å b: 88.154Å c: 85.512Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.162 0.16 0.191
Expression system: Escherichia coli BL21(DE3)