6TOR

human O-phosphoethanolamine phospho-lyase


Experimental Data Snapshot

  • Method: X-RAY DIFFRACTION
  • Resolution: 2.05 Å
  • R-Value Free: 0.199 
  • R-Value Work: 0.163 
  • R-Value Observed: 0.165 

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Ligand Structure Quality Assessment 


This is version 1.2 of the entry. See complete history


Literature

Structural characterization of human O-phosphoethanolamine phospho-lyase.

Vettraino, C.Peracchi, A.Donini, S.Parisini, E.

(2020) Acta Crystallogr F Struct Biol Commun 76: 160-167

  • DOI: https://doi.org/10.1107/S2053230X20002988
  • Primary Citation of Related Structures:  
    6TOR

  • PubMed Abstract: 

    Human O-phosphoethanolamine phospho-lyase (hEtnppl; EC 4.2.3.2) is a pyridoxal 5'-phosphate-dependent enzyme that catalyzes the degradation of O-phosphoethanolamine (PEA) into acetaldehyde, phosphate and ammonia. Physiologically, the enzyme is involved in phospholipid metabolism, as PEA is the precursor of phosphatidylethanolamine in the CDP-ethanolamine (Kennedy) pathway. Here, the crystal structure of hEtnppl in complex with pyridoxamine 5'-phosphate was determined at 2.05 Å resolution by molecular replacement using the structure of A1RDF1 from Arthrobacter aurescens TC1 (PDB entry 5g4i) as the search model. Structural analysis reveals that the two proteins share the same general fold and a similar arrangement of active-site residues. These results provide novel and useful information for the complete characterization of the human enzyme.


  • Organizational Affiliation

    Center for Nano Science and Technology @PoliMi, Istituto Italiano di Tecnologia, Via Pascoli 70/3, 20133 Milano, Italy.


Macromolecules
Find similar proteins by:  (by identity cutoff)  |  3D Structure
Entity ID: 1
MoleculeChains Sequence LengthOrganismDetailsImage
Ethanolamine-phosphate phospho-lyase
A, B
499Homo sapiensMutation(s): 0 
Gene Names: ETNPPLAGXT2L1
EC: 4.2.3.2
UniProt & NIH Common Fund Data Resources
Find proteins for Q8TBG4 (Homo sapiens)
Explore Q8TBG4 
Go to UniProtKB:  Q8TBG4
PHAROS:  Q8TBG4
GTEx:  ENSG00000164089 
Entity Groups  
Sequence Clusters30% Identity50% Identity70% Identity90% Identity95% Identity100% Identity
UniProt GroupQ8TBG4
Sequence Annotations
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  • Reference Sequence
Experimental Data & Validation

Experimental Data

  • Method: X-RAY DIFFRACTION
  • Resolution: 2.05 Å
  • R-Value Free: 0.199 
  • R-Value Work: 0.163 
  • R-Value Observed: 0.165 
  • Space Group: H 3
Unit Cell:
Length ( Å )Angle ( ˚ )
a = 137.998α = 90
b = 137.998β = 90
c = 121.87γ = 120
Software Package:
Software NamePurpose
REFMACrefinement
PHASERmodel building
SCALAdata scaling
MOSFLMdata processing
XDSdata reduction
PHASERphasing

Structure Validation

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Ligand Structure Quality Assessment 


Entry History 

Deposition Data

Revision History  (Full details and data files)

  • Version 1.0: 2020-04-15
    Type: Initial release
  • Version 1.1: 2020-04-22
    Changes: Database references
  • Version 1.2: 2024-01-24
    Changes: Data collection, Database references, Refinement description