› 3c9s

X-ray diffraction
2.2Å resolution

AaThiL complexed with AMPPCP

Released:
DOI: 10.2210/pdb3c9s/pdb
PDB entry 3c9s coloured by chain, front view.
PDB entry 3c9s coloured by chain, side view.
PDB entry 3c9s coloured by chain, top view.
Source organism: Aquifex aeolicus
Primary publication:
Structural studies of thiamin monophosphate kinase in complex with substrates and products.
McCulloch KM, Kinsland C, Begley TP, Ealick SE
Biochemistry 47 3810-21 (2008)
PMID: 18311927

Function and Biology Details

Reaction catalysed: 
ATP + thiamine phosphate = ADP + thiamine diphosphate
Biochemical function:
Biological process:
Cellular component:
  • not assigned
Sequence domains:
Structure domains:

Structure analysis Details

Assembly composition:
homo dimer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-130581 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Thiamine-monophosphate kinase Chains: A, B
Molecule details ›
Chains: A, B
Length: 342 amino acids
Theoretical weight: 38.47 KDa
Source organism: Aquifex aeolicus
Expression system: Escherichia coli
UniProt:
  • Canonical: O67883 (Residues: 1-306; Coverage: 100%)
Gene names: aq_2119, thiL
Sequence domains: AIR synthase related protein, N-terminal domain
Structure domains:

Ligands and Environments

2 bound ligands:
Ligand MG 6 x MG
Ligand ACP 2 x ACP
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: APS BEAMLINE 24-ID-C
Spacegroup: P212121
Unit cell:
a: 61.204Å b: 67.137Å c: 203.472Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.217 0.217 0.256
Expression system: Escherichia coli

Quick links

Citations

3 review citations

The structural and biochemical foundations of thiamin biosynthesis.
Jurgenson et al. (2009)
2 more

2 mentions without citation

Structural studies of thiamin monophosphate kinase in complex with substrates and products.
McCulloch et al. (2008)
1 more