› 6tor

X-ray diffraction
2.05Å resolution

human O-phosphoethanolamine phospho-lyase

Released:
DOI: 10.2210/pdb6tor/pdb
PDB entry 6tor coloured by chain, front view.
PDB entry 6tor coloured by chain, side view.
PDB entry 6tor coloured by chain, top view.
Source organism: Homo sapiens
Primary publication:
Structural characterization of human O-phosphoethanolamine phospho-lyase.
Vettraino C, Peracchi A, Donini S, Parisini E
Acta Crystallogr F Struct Biol Commun 76 160-167 (2020)
PMID: 32254049

Function and Biology Details

Reaction catalysed: 
Ethanolamine phosphate + H(2)O = acetaldehyde + NH(3) + phosphate
Biochemical function:
Biological process:
  • not assigned
Cellular component:
Sequence domains:

Structure analysis Details

Assembly composition:
homo dimer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-186179 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Ethanolamine-phosphate phospho-lyase Chains: A, B
Molecule details ›
Chains: A, B
Length: 499 amino acids
Theoretical weight: 55.76 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
UniProt:
  • Canonical: Q8TBG4 (Residues: 1-499; Coverage: 100%)
Gene names: AGXT2L1, ETNPPL
Sequence domains: Aminotransferase class-III

Ligands and Environments


Cofactor: Ligand PMP 2 x PMP
1 bound ligand:
Ligand GOL 6 x GOL
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: SLS BEAMLINE X06DA
Spacegroup: R3
Unit cell:
a: 137.998Å b: 137.998Å c: 121.87Å
α: 90° β: 90° γ: 120°
R-values:
R R work R free
0.165 0.163 0.199
Expression system: Escherichia coli

Quick links

Citations

1 mention without citation

Structural characterization of human O-phosphoethanolamine phospho-lyase.
Vettraino et al. (2020)