› 4muy

X-ray diffraction
1.8Å resolution

IspH in complex with pyridin-4-ylmethyl diphosphate

Released:
DOI: 10.2210/pdb4muy/pdb
PDB 4muy coloured by chain and viewed from the front.
PDB 4muy coloured by chain and viewed from the side.
PDB 4muy coloured by chain and viewed from the top.
Source organism: Escherichia coli K-12
Primary publication:
Insights into the binding of pyridines to the iron-sulfur enzyme IspH.
Span I, Wang K, Eisenreich W, Bacher A, Zhang Y, Oldfield E, Groll M
OpenAccess logo J Am Chem Soc 136 7926-32 (2014)
PMID: 24813236

Function and Biology Details

Biochemical function:
  • not assigned
Biological process:
  • not assigned
Cellular component:
  • not assigned
Sequence domain:

Structure analysis Details

Assembly composition:
monomeric (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
4-hydroxy-3-methylbut-2-enyl diphosphate reductase Chains: A, B
Molecule details ›
Chains: A, B
Length: 327 amino acids
Theoretical weight: 36.11 KDa
Source organism: Escherichia coli K-12
Expression system: Escherichia coli
Structure domains:

Ligands and Environments

2 bound ligands:
Ligand F3S 2 x F3S
Ligand 2E5 2 x 2E5
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: SLS BEAMLINE X06SA
Spacegroup: P212121
Unit cell:
a: 70.19Å b: 80.46Å c: 110.89Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.179 0.177 0.224
Expression system: Escherichia coli

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Citations

1 review citation

Advanced paramagnetic resonance spectroscopies of iron-sulfur proteins: Electron nuclear double resonance (ENDOR) and electron spin echo envelope modulation (ESEEM).
Cutsail et al. (2015)
4 other articles

2 mentions without citation

Insights into the binding of pyridines to the iron-sulfur enzyme IspH.
Span et al. (2014)
1 more