PDBe 2jg2

X-ray diffraction
1.3Å resolution

HIGH RESOLUTION STRUCTURE OF SPT WITH PLP INTERNAL ALDIMINE

Released:

Function and Biology Details

Reaction catalysed:
Palmitoyl-CoA + L-serine = CoA + 3-dehydro-D-sphinganine + CO(2)
Biochemical function:
Biological process:
  • not assigned
Cellular component:
  • not assigned

Structure analysis Details

Assembly composition:
homo dimer (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Aminotransferase class I/II-fold pyridoxal phosphate-dependent enzyme Chain: A
Molecule details ›
Chain: A
Length: 422 amino acids
Theoretical weight: 45.33 KDa
Source organism: Sphingomonas paucimobilis
Expression system: Escherichia coli
UniProt:
  • Canonical: Q93UV0 (Residues: 1-420; Coverage: 100%)
Gene names: DRN02_00350, SPT1
Sequence domains: Aminotransferase class I and II

Ligands and Environments


Cofactor: Ligand PLP 1 x PLP
1 bound ligand:

No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: ESRF BEAMLINE BM14
Spacegroup: C2221
Unit cell:
a: 74.19Å b: 107.552Å c: 90.322Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.155 0.153 0.185
Expression system: Escherichia coli