PDBe 1e51

X-ray diffraction
2.83Å resolution

Crystal structure of native human erythrocyte 5-aminolaevulinic acid dehydratase

Released:
Source organism: Homo sapiens
Entry authors: Mills-Davies NL, Thompson D, Cooper JB, Shoolingin-Jordan PM

Function and Biology Details

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

Structure analysis Details

Assembly composition:
homo octamer (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: 36.34 KDa
Source organism: Homo sapiens
UniProt:
  • Canonical: P13716 (Residues: 1-330; Coverage: 100%)
Gene name: ALAD
Sequence domains: Delta-aminolevulinic acid dehydratase
Structure domains: Aldolase class I

Ligands and Environments

3 bound ligands:

No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: SRS BEAMLINE PX9.5
Spacegroup: I422
Unit cell:
a: 125.53Å b: 125.53Å c: 200.91Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.213 0.213 0.27