PDBe 1pv8

X-ray diffraction
2.2Å resolution

Crystal structure of a low activity F12L mutant of human porphobilinogen synthase

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 hexamer (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: 36.3 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
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

2 bound ligands:

No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: RIGAKU RU200
Spacegroup: P63
Unit cell:
a: 89.571Å b: 89.571Å c: 153.19Å
α: 90° β: 90° γ: 120°
R-values:
R R work R free
0.21 0.199 0.284
Expression system: Escherichia coli