› 5lzl

X-ray diffraction
3.47Å resolution

Function and Biology Details

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

Structure analysis Details

Assembly composition:
homo octamer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-107193 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Delta-aminolevulinic acid dehydratase Chains: A, B, C, D, E, F, G, H, I, J, K, L
Molecule details ›
Chains: A, B, C, D, E, F, G, H, I, J, K, L
Length: 338 amino acids
Theoretical weight: 37.72 KDa
Source organism: Pyrobaculum calidifontis JCM 11548
Expression system: Escherichia coli
UniProt:
  • Canonical: A3MWV9 (Residues: 1-338; Coverage: 100%)
Gene name: Pcal_1709
Sequence domains: Delta-aminolevulinic acid dehydratase
Structure domains: Aldolase class I

Ligands and Environments

1 bound ligand:
Ligand ZN 24 x ZN
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: DIAMOND BEAMLINE I02
Spacegroup: P3121
Unit cell:
a: 205.561Å b: 205.561Å c: 199.171Å
α: 90° β: 90° γ: 120°
R-values:
R R work R free
0.153 0.148 0.25
Expression system: Escherichia coli

Quick links

Citations

3 review citations

Organoselenium compounds as mimics of selenoproteins and thiol modifier agents.
Barbosa et al. (2017)
2 more

1 mention without citation

The Se…S/N interactions as a possible mechanism of δ-aminolevulinic acid dehydratase enzyme inhibition by organoselenium compounds: A computational study.
Nogara et al. (2020)