› 5hms

X-ray diffraction
2.8Å resolution

X-ray structure of human recombinant 5-aminolaevulinic acid dehydratase (hrALAD).

Released:
DOI: 10.2210/pdb5hms/pdb
PDB entry 5hms coloured by chain, front view.
PDB entry 5hms coloured by chain, side view.
PDB entry 5hms coloured by chain, top view.
Source organism: Homo sapiens
Primary publication:
Structural studies of substrate and product complexes of 5-aminolaevulinic acid dehydratase from humans, Escherichia coli and the hyperthermophile Pyrobaculum calidifontis.
Mills-Davies N, Butler D, Norton E, Thompson D, Sarwar M, Guo J, Gill R, Azim N, Coker A, Wood SP, Erskine PT, Coates L, Cooper JB, Rashid N, Akhtar M, Shoolingin-Jordan PM
Acta Crystallogr D Struct Biol 73 9-21 (2017)
PMID: 28045381

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-146722 (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: 36.34 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli BL21(DE3)
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

1 bound ligand:
Ligand ZN 2 x ZN
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: ESRF BEAMLINE ID14-2
Spacegroup: P4212
Unit cell:
a: 127.079Å b: 127.079Å c: 91.231Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.177 0.172 0.265
Expression system: Escherichia coli BL21(DE3)

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Citations

3 review citations

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