› 3ll5

X-ray diffraction
1.99Å resolution

Crystal structure of T. acidophilum isopentenyl phosphate kinase product complex

Released:
DOI: 10.2210/pdb3ll5/pdb
PDB entry 3ll5 coloured by chain, front view.
PDB entry 3ll5 coloured by chain, side view.
PDB entry 3ll5 coloured by chain, top view.
Source organism: Thermoplasma acidophilum DSM 1728
Primary publication:
X-ray structures of isopentenyl phosphate kinase.
Mabanglo MF, Schubert HL, Chen M, Hill CP, Poulter CD
ACS Chem Biol 5 517-27 (2010)
PMID: 20402538

Function and Biology Details

Reaction catalysed: 
ATP + 3-methylbut-3-en-1-yl phosphate = ADP + 3-methylbut-3-en-1-yl diphosphate
Biochemical function:
Biological process:
Cellular component:
Sequence domains:

Structure analysis Details

Assembly composition:
homo dimer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-190903 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Isopentenyl phosphate kinase Chains: A, B, C, D
Molecule details ›
Chains: A, B, C, D
Length: 249 amino acids
Theoretical weight: 28.11 KDa
Source organism: Thermoplasma acidophilum DSM 1728
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: Q9HLX1 (Residues: 1-245; Coverage: 100%)
Gene name: Ta0103
Sequence domains: Amino acid kinase family
Structure domains: Acetylglutamate kinase-like

Ligands and Environments

4 bound ligands:
Ligand ADP 2 x ADP
Ligand IPE 2 x IPE
Ligand ATP 2 x ATP
Ligand IP8 2 x IP8
1 modified residue:
Ligand MSE 48 x MSE

Experiments and Validation Details

Entry percentile scores
X-ray source: SSRL BEAMLINE BL11-1
Spacegroup: C2
Unit cell:
a: 187.104Å b: 42.787Å c: 134.895Å
α: 90° β: 113.19° γ: 90°
R-values:
R R work R free
0.195 0.193 0.238
Expression system: Escherichia coli BL21(DE3)

Quick links

Citations

5 review citations

Enzymes of the mevalonate pathway of isoprenoid biosynthesis.
Miziorko HM. (2011)
4 more

4 mentions without citation

X-ray structures of isopentenyl phosphate kinase.
Mabanglo et al. (2010)
3 more