6hrh

X-ray diffraction
2.3Å resolution

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

Released:
Source organism: Homo sapiens
Entry authors: Bailey HJ, 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 WW, Structural Genomics Consortium (SGC)

Function and Biology Details

Structure analysis Details

Assembly composition:
homo dimer (preferred)
PDBe Complex ID:
PDB-CPX-149672 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
5-aminolevulinate synthase, erythroid-specific, mitochondrial Chains: A, B
Molecule details ›
Chains: A, B
Length: 469 amino acids
Theoretical weight: 52.25 KDa
Source organism: Homo sapiens
Expression system: Spodoptera frugiperda
UniProt:
  • Canonical: P22557 (Residues: 143-587; Coverage: 76%)
Gene names: ALAS2, ALASE, ASB
Sequence domains: Aminotransferase class I and II

Ligands and Environments


Cofactor: Ligand PLP 2 x PLP
No bound ligands
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: DIAMOND BEAMLINE I04
Spacegroup: C2
Unit cell:
a: 125.771Å b: 107.703Å c: 75.713Å
α: 90° β: 109.05° γ: 90°
R-values:
R R work R free
0.214 0.213 0.234
Expression system: Spodoptera frugiperda