› 1aw5

X-ray diffraction
2.3Å resolution

5-AMINOLEVULINATE DEHYDRATASE FROM SACCHAROMYCES CEREVISIAE

Released:
DOI: 10.2210/pdb1aw5/pdb
PDB entry 1aw5 coloured by chain, front view.
PDB entry 1aw5 coloured by chain, side view.
PDB entry 1aw5 coloured by chain, top view.
Source organism: Saccharomyces cerevisiae
Primary publication:
X-ray structure of 5-aminolaevulinate dehydratase, a hybrid aldolase.
Erskine PT, Senior N, Awan S, Lambert R, Lewis G, Tickle IJ, Sarwar M, Spencer P, Thomas P, Warren MJ, Shoolingin-Jordan PM, Wood SP, Cooper JB
Nat Struct Biol 4 1025-31 (1997)
PMID: 9406553

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-138644 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Delta-aminolevulinic acid dehydratase Chain: A
Molecule details ›
Chain: A
Length: 340 amino acids
Theoretical weight: 37.62 KDa
Source organism: Saccharomyces cerevisiae
Expression system: Escherichia coli
UniProt:
  • Canonical: P05373 (Residues: 1-340; Coverage: 99%)
Gene names: HEM2, YGL040C
Sequence domains: Delta-aminolevulinic acid dehydratase
Structure domains: Aldolase class I

Ligands and Environments

1 bound ligand:
Ligand ZN 2 x ZN
1 modified residue:
Ligand MSE 5 x MSE

Experiments and Validation Details

Entry percentile scores
X-ray source: ESRF BEAMLINE BM14
Spacegroup: I422
Unit cell:
a: 102.5Å b: 102.5Å c: 168.3Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.198 not available 0.27
Expression system: Escherichia coli

Quick links

Citations

20 review citations

Antimicrobial activity of metals: mechanisms, molecular targets and applications.
Lemire et al. (2013)
19 more

1 mention without citation

Crystal structure of Toxoplasma gondii porphobilinogen synthase: insights on octameric structure and porphobilinogen formation.
Jaffe et al. (2011)