› 2g1k

X-ray diffraction
1.75Å resolution

Crystal structure of Mycobacterium tuberculosis shikimate kinase in complex with shikimate at 1.75 angstrom resolution

Released:
DOI: 10.2210/pdb2g1k/pdb
PDB entry 2g1k coloured by chain, front view.
PDB entry 2g1k coloured by chain, side view.
PDB entry 2g1k coloured by chain, top view.
Source organism: Mycobacterium tuberculosis
Primary publication:
Crystal structure of Mycobacterium tuberculosis shikimate kinase in complex with shikimic acid and an ATP analogue.
Gan J, Gu Y, Li Y, Yan H, Ji X
Biochemistry 45 8539-45 (2006)
PMID: 16834327

Function and Biology Details

Reaction catalysed: 
ATP + shikimate = ADP + shikimate 3-phosphate
Biochemical function:
Biological process:
Cellular component:
Sequence domains:
Structure domain:

Structure analysis Details

Assembly composition:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-552451 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Shikimate kinase Chain: A
Molecule details ›
Chain: A
Length: 176 amino acids
Theoretical weight: 18.61 KDa
Source organism: Mycobacterium tuberculosis
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: P9WPY3 (Residues: 1-176; Coverage: 100%)
Gene names: MTCY159.17, Rv2539c, aroK
Sequence domains: Shikimate kinase
Structure domains: P-loop containing nucleotide triphosphate hydrolases

Ligands and Environments

3 bound ligands:
Ligand SO4 3 x SO4
Ligand CL 2 x CL
Ligand SKM 1 x SKM
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: APS BEAMLINE 22-ID
Spacegroup: P3121
Unit cell:
a: 59.309Å b: 59.309Å c: 102.537Å
α: 90° β: 90° γ: 120°
R-values:
R R work R free
0.223 0.222 0.247
Expression system: Escherichia coli BL21(DE3)

Quick links

Citations

1 review citation

The shikimate pathway and aromatic amino Acid biosynthesis in plants.
Maeda et al. (2012)
23 other articles

2 mentions without citation

Selective Mycobacterium tuberculosis Shikimate Kinase Inhibitors as Potential Antibacterials.
Gordon et al. (2015)
1 more