› 3c9t

X-ray diffraction
2.6Å resolution

AaThiL complexed with AMPPCP and TMP

Released:
DOI: 10.2210/pdb3c9t/pdb
PDB entry 3c9t coloured by chain, front view.
PDB entry 3c9t coloured by chain, side view.
PDB entry 3c9t 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

3 bound ligands:
Ligand MG 10 x MG
Ligand TPS 2 x TPS
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: 60.75Å b: 66.843Å c: 196.86Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.213 0.213 0.27
Expression system: Escherichia coli

Quick links

Citations

1 review citation

Thiamin biosynthesis: still yielding fascinating biological chemistry.
Begley et al. (2012)
13 other articles

8 mentions without citation

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