› 5lqq

X-ray diffraction
2.4Å resolution

Function and Biology Details

Reactions catalysed: 
1-alkyl-sn-glycero-3-phosphoethanolamine + H(2)O = 1-alkyl-sn-glycerol 3-phosphate + ethanolamine
A phosphatidylcholine + H(2)O = choline + a phosphatidate
Biochemical function:
Biological process:
Cellular component:
Sequence domains:

Structure analysis Details

Assembly composition:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-179148 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecules (2 distinct):
Autotaxin Chain: A
Molecule details ›
Chain: A
Length: 827 amino acids
Theoretical weight: 95.04 KDa
Source organism: Rattus norvegicus
Expression system: Homo sapiens
UniProt:
  • Canonical: Q64610 (Residues: 36-887; Coverage: 96%)
  • Best match: Q64610-2 (Residues: 36-862)
Gene names: Atx, Enpp2, Npps2
Sequence domains:
Structure domains:

Ligands and Environments

Carbohydrate polymer : NEW Components: NAG, BMA, MAN
Carbohydrate polymer
5 bound ligands:
Ligand ZN 2 x ZN
Ligand CA 1 x CA
Ligand IOD 10 x IOD
Ligand 72P 1 x 72P
Ligand NA 1 x NA
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: SLS BEAMLINE X06DA
Spacegroup: P21
Unit cell:
a: 62.655Å b: 89.067Å c: 77.509Å
α: 90° β: 102.88° γ: 90°
R-values:
R R work R free
0.219 0.217 0.262
Expression system: Homo sapiens

Quick links

Citations

3 review citations

Design and Development of Autotaxin Inhibitors.
Jia et al. (2021)
2 more

3 mentions without citation

The Structural Binding Mode of the Four Autotaxin Inhibitor Types that Differentially Affect Catalytic and Non-Catalytic Functions.
Salgado-Polo et al. (2019)
2 more