6HRH

Structure of human erythroid-specific 5'-aminolevulinate synthase, ALAS2


Experimental Data Snapshot

  • Method: X-RAY DIFFRACTION
  • Resolution: 2.30 Å
  • R-Value Free: 0.234 
  • R-Value Work: 0.213 
  • R-Value Observed: 0.214 

wwPDB Validation   3D Report Full Report


Ligand Structure Quality Assessment 


This is version 1.1 of the entry. See complete history


Literature

Structure of human erythroid-specific 5'-aminolevulinate synthase, ALAS2

Bailey, H.J.Shrestha, L.Rembeza, E.Newman, J.Kupinska, K.Diaz-saez, L.Kennedy, E.Burgess-Brown, N.von Delft, F.Arrowsmith, C.Edwards, A.Bountra, C.Yue, W.W.

To be published.

Macromolecules
Find similar proteins by:  (by identity cutoff)  |  3D Structure
Entity ID: 1
MoleculeChains Sequence LengthOrganismDetailsImage
5-aminolevulinate synthase, erythroid-specific, mitochondrialA [auth B],
B [auth A]
469Homo sapiensMutation(s): 0 
Gene Names: ALAS2ALASEASB
EC: 2.3.1.37
UniProt & NIH Common Fund Data Resources
Find proteins for P22557 (Homo sapiens)
Explore P22557 
Go to UniProtKB:  P22557
PHAROS:  P22557
GTEx:  ENSG00000158578 
Entity Groups  
Sequence Clusters30% Identity50% Identity70% Identity90% Identity95% Identity100% Identity
UniProt GroupP22557
Sequence Annotations
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  • Reference Sequence
Small Molecules
Experimental Data & Validation

Experimental Data

  • Method: X-RAY DIFFRACTION
  • Resolution: 2.30 Å
  • R-Value Free: 0.234 
  • R-Value Work: 0.213 
  • R-Value Observed: 0.214 
  • Space Group: C 1 2 1
Unit Cell:
Length ( Å )Angle ( ˚ )
a = 125.771α = 90
b = 107.703β = 109.05
c = 75.713γ = 90
Software Package:
Software NamePurpose
xia2data scaling
PHASERphasing
PHENIXrefinement
PDB_EXTRACTdata extraction
DIALSdata reduction

Structure Validation

View Full Validation Report



Ligand Structure Quality Assessment 


Entry History 

Revision History  (Full details and data files)

  • Version 1.0: 2018-11-07
    Type: Initial release
  • Version 1.1: 2024-01-24
    Changes: Data collection, Database references, Refinement description