2pt5

X-ray diffraction
2.1Å resolution

Crystal Structure Of Shikimate Kinase (aq_2177) From Aquifex Aeolicus vf5

Released:
Source organism: Aquifex aeolicus VF5
Entry authors: Jeyakanthan J, Nithya N, Shimada A, Velmurugan D, Ebihara A, Shinkai A, Kuramitsu S, Shiro Y, Yokoyama S, RIKEN Structural Genomics/Proteomics Initiative (RSGI)

Function and Biology Details

Reaction catalysed:
ATP + shikimate = ADP + shikimate 3-phosphate
Biochemical function:
Cellular component:

Structure analysis Details

Assemblies composition:
monomeric (preferred)
homo dimer
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Shikimate kinase Chains: A, B, C, D
Molecule details ›
Chains: A, B, C, D
Length: 168 amino acids
Theoretical weight: 19.25 KDa
Source organism: Aquifex aeolicus VF5
Expression system: Escherichia coli
UniProt:
  • Canonical: O67925 (Residues: 1-168; Coverage: 100%)
Gene names: aq_2177, aroK
Sequence domains: Shikimate kinase
Structure domains: P-loop containing nucleotide triphosphate hydrolases

Ligands and Environments

2 bound ligands:
1 modified residue:

Experiments and Validation Details

Entry percentile scores
X-ray source: SPRING-8 BEAMLINE BL26B2
Spacegroup: P21
Unit cell:
a: 51.598Å b: 57.932Å c: 97.143Å
α: 90° β: 90.59° γ: 90°
R-values:
R R work R free
0.214 0.214 0.269
Expression system: Escherichia coli