PDBe 5hms

X-ray diffraction
2.8Å resolution

X-ray structure of human recombinant 5-aminolaevulinic acid dehydratase (hrALAD).

Released:

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
Expression system: Escherichia coli BL21(DE3)
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

1 bound ligand:

No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: ESRF BEAMLINE ID14-2
Spacegroup: P4212
Unit cell:
a: 127.079Å b: 127.079Å c: 91.231Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.177 0.172 0.265
Expression system: Escherichia coli BL21(DE3)