› 2w8t

X-ray diffraction
1.25Å resolution

Function and Biology Details

Reaction catalysed: 
Palmitoyl-CoA + L-serine = CoA + 3-dehydro-D-sphinganine + CO(2)
Biochemical function:
Biological process:
Cellular component:
Sequence domains:

Structure analysis Details

Assembly composition:
homo dimer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-188138 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Serine palmitoyltransferase Chain: A
Molecule details ›
Chain: A
Length: 427 amino acids
Theoretical weight: 46.02 KDa
Source organism: Sphingomonas paucimobilis
Expression system: Escherichia coli
UniProt:
  • Canonical: Q93UV0 (Residues: 2-420; Coverage: 100%)
Gene names: HKX06_04505, I6G38_17245, SPT1, spt
Sequence domains: Aminotransferase class I and II
Structure domains:

Ligands and Environments


Cofactor: Ligand PLP 1 x PLP
No bound ligands
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: ESRF BEAMLINE ID14-4
Spacegroup: C2221
Unit cell:
a: 75.18Å b: 107.454Å c: 88.825Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.15 0.149 0.165
Expression system: Escherichia coli

Quick links

Citations

5 review citations

Sphingolipid and glycosphingolipid metabolic pathways in the era of sphingolipidomics.
Merrill AH. (2011)
4 more

3 mentions without citation

Sphingolipid biosynthesis in man and microbes.
Harrison et al. (2018)
2 more