› 1qml

X-ray diffraction
3Å resolution

Hg complex of yeast 5-aminolaevulinic acid dehydratase

Released:
DOI: 10.2210/pdb1qml/pdb
PDB entry 1qml coloured by chain, front view.
PDB entry 1qml coloured by chain, side view.
PDB entry 1qml coloured by chain, top view.
Source organism: Saccharomyces cerevisiae
Primary publication:
MAD analyses of yeast 5-aminolaevulinate dehydratase: their use in structure determination and in defining the metal-binding sites.
Erskine PT, Duke EM, Tickle IJ, Senior NM, Warren MJ, Cooper JB
Acta Crystallogr D Biol Crystallogr 56 421-30 (2000)
PMID: 10739915

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: 342 amino acids
Theoretical weight: 37.79 KDa
Source organism: Saccharomyces cerevisiae
UniProt:
  • Canonical: P05373 (Residues: 1-342; Coverage: 100%)
Gene names: HEM2, YGL040C
Sequence domains: Delta-aminolevulinic acid dehydratase
Structure domains: Aldolase class I

Ligands and Environments

1 bound ligand:
Ligand HG 1 x HG
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: SRS BEAMLINE PX9.6
Spacegroup: I422
Unit cell:
a: 102.05Å b: 102.05Å c: 170.49Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.249 0.249 0.33

Quick links

Citations

1 review citation

Protein design: toward functional metalloenzymes.
Yu et al. (2014)
15 other articles

1 mention without citation

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