› 1e6c

X-ray diffraction
1.8Å resolution

K15M MUTANT OF SHIKIMATE KINASE FROM ERWINIA CHRYSANTHEMI

Released:
DOI: 10.2210/pdb1e6c/pdb
PDB entry 1e6c coloured by chain, front view.
PDB entry 1e6c coloured by chain, side view.
PDB entry 1e6c coloured by chain, top view.
Source organism: Dickeya chrysanthemi
Primary publication:
Biochemical and X-ray crystallographic studies on shikimate kinase: the important structural role of the P-loop lysine.
Krell T, Maclean J, Boam DJ, Cooper A, Resmini M, Brocklehurst K, Kelly SM, Price NC, Lapthorn AJ, Coggins JR
Protein Sci 10 1137-49 (2001)
PMID: 11369852

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-145505 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Shikimate kinase 2 Chains: A, B
Molecule details ›
Chains: A, B
Length: 173 amino acids
Theoretical weight: 18.99 KDa
Source organism: Dickeya chrysanthemi
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: P10880 (Residues: 1-173; Coverage: 100%)
Gene names: aroL, aroM
Sequence domains: Shikimate kinase
Structure domains: P-loop containing nucleotide triphosphate hydrolases

Ligands and Environments

4 bound ligands:
Ligand PO4 2 x PO4
Ligand CL 2 x CL
Ligand MPD 5 x MPD
Ligand MRD 1 x MRD
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: SRS BEAMLINE PX9.6
Spacegroup: P21
Unit cell:
a: 42.86Å b: 106.94Å c: 42.75Å
α: 90° β: 119.96° γ: 90°
R-values:
R R work R free
0.188 0.188 0.227
Expression system: Escherichia coli BL21(DE3)

Quick links

Citations

3 review citations

Structural biology and drug discovery of difficult targets: the limits of ligandability.
Surade et al. (2012)
2 more

3 mentions without citation

Biochemical and X-ray crystallographic studies on shikimate kinase: the important structural role of the P-loop lysine.
Krell et al. (2001)
2 more