2z0i

X-ray diffraction
3.2Å resolution

Crystal Structure of 5-aminolevulinic acid dehydratase (ALAD) from Mus musculus

Released:
Source organism: Mus musculus
Entry authors: Wang H, Xie Y, Kawazoe M, Kishishita S, Murayama K, Takemoto C, Terada T, Shirouzu M, Yokoyama S, RIKEN Structural Genomics/Proteomics Initiative (RSGI)

Function and Biology Details

Reaction catalysed:
2 5-aminolevulinate = porphobilinogen + 2 H(2)O
Biochemical function:
Cellular component:

Structure analysis Details

Assemblies composition:
homo dimer (preferred)
homo octamer
PDBe Complex ID:
PDB-CPX-145331 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Delta-aminolevulinic acid dehydratase Chains: A, B
Molecule details ›
Chains: A, B
Length: 330 amino acids
Theoretical weight: 36.55 KDa
Source organism: Mus musculus
Expression system: Cell-free protein synthesis
UniProt:
  • Canonical: P10518 (Residues: 1-330; Coverage: 100%)
Gene names: Alad, Lv
Sequence domains: Delta-aminolevulinic acid dehydratase
Structure domains: Aldolase class I

Ligands and Environments

No bound ligands
1 modified residue:

Experiments and Validation Details

Entry percentile scores
X-ray source: PHOTON FACTORY BEAMLINE BL-5A
Spacegroup: I422
Unit cell:
a: 121.51Å b: 121.51Å c: 196.7Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.233 0.233 0.269
Expression system: Cell-free protein synthesis