› 1q0q

X-ray diffraction
1.9Å resolution

Function and Biology Details

Reaction catalysed: 
2-C-methyl-D-erythritol 4-phosphate + NADP(+) = 1-deoxy-D-xylulose 5-phosphate + NADPH
Biochemical function:
Biological process:
Cellular component:
Sequence domains:
Structure domains:

Structure analysis Details

Assembly composition:
homo dimer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-155316 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
1-deoxy-D-xylulose 5-phosphate reductoisomerase Chains: A, B
Molecule details ›
Chains: A, B
Length: 406 amino acids
Theoretical weight: 44.4 KDa
Source organism: Escherichia coli
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: P45568 (Residues: 1-398; Coverage: 100%)
Gene names: JW0168, b0173, dxr, ispC, yaeM
Sequence domains:
Structure domains:

Ligands and Environments


Cofactor: Ligand NDP 2 x NDP
1 bound ligand:
Ligand DXP 2 x DXP
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: SLS BEAMLINE X06SA
Spacegroup: C2221
Unit cell:
a: 107.057Å b: 122.846Å c: 128.553Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.177 0.174 0.212
Expression system: Escherichia coli BL21(DE3)

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Citations

14 review citations

Co-operation of TLR4 and raft proteins in LPS-induced pro-inflammatory signaling.
Płóciennikowska et al. (2015)
13 more

6 mentions without citation

Structure of 1-deoxy-D-xylulose 5-phosphate reductoisomerase in a quaternary complex with a magnesium ion, NADPH and the antimalarial drug fosmidomycin.
Yajima et al. (2007)
5 more