› 1i8j

X-ray diffraction
1.9Å resolution

CRYSTAL STRUCTURE OF PORPHOBILINOGEN SYNTHASE COMPLEXED WITH THE INHIBITOR 4,7-DIOXOSEBACIC ACID

Released:
DOI: 10.2210/pdb1i8j/pdb
PDB entry 1i8j coloured by chain, front view.
PDB entry 1i8j coloured by chain, side view.
PDB entry 1i8j coloured by chain, top view.
Source organism: Escherichia coli
Primary publication:
Mechanistic basis for suicide inactivation of porphobilinogen synthase by 4,7-dioxosebacic acid, an inhibitor that shows dramatic species selectivity.
Kervinen J, Jaffe EK, Stauffer F, Neier R, Wlodawer A, Zdanov A
Biochemistry 40 8227-36 (2001)
PMID: 11444968

Function and Biology Details

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

Structure analysis Details

Assembly composition:
homo octamer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-142257 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Delta-aminolevulinic acid dehydratase Chains: A, B
Molecule details ›
Chains: A, B
Length: 323 amino acids
Theoretical weight: 35.54 KDa
Source organism: Escherichia coli
Expression system: Escherichia coli
UniProt:
  • Canonical: P0ACB2 (Residues: 2-324; Coverage: 100%)
Gene names: JW0361, b0369, hemB, ncf
Sequence domains: Delta-aminolevulinic acid dehydratase
Structure domains: Aldolase class I

Ligands and Environments

3 bound ligands:
Ligand ZN 2 x ZN
Ligand MG 2 x MG
Ligand DSB 2 x DSB
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: RIGAKU RU200
Spacegroup: P4212
Unit cell:
a: 128.741Å b: 128.741Å c: 142.76Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.198 0.198 0.247
Expression system: Escherichia coli

Quick links

Citations

5 review citations

The biochemistry of heme biosynthesis.
Heinemann et al. (2008)
4 more

4 mentions without citation

Moonlighting Proteins in the Fuzzy Logic of Cellular Metabolism.
Liu et al. (2020)
3 more