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TitleStructural studies of substrate and product complexes of 5-aminolaevulinic acid dehydratase from humans, Escherichia coli and the hyperthermophile Pyrobaculum calidifontis.
Journal, issue, pagesActa Crystallogr D Struct Biol, Vol. 73, Page 9-21, Year 2017
Publish dateJan 17, 2016 (structure data deposition date)
AuthorsMills-Davies, N. / Butler, D. / Norton, E. / Thompson, D. / Sarwar, M. / Guo, J. / Gill, R. / Azim, N. / Coker, A. / Wood, S.P. ...Mills-Davies, N. / Butler, D. / Norton, E. / Thompson, D. / Sarwar, M. / Guo, J. / Gill, R. / Azim, N. / Coker, A. / Wood, S.P. / Erskine, P.T. / Coates, L. / Cooper, J.B. / Rashid, N. / Akhtar, M. / Shoolingin-Jordan, P.M.
External linksActa Crystallogr D Struct Biol / PubMed:28045381
MethodsX-ray diffraction
Resolution2.1 - 3.47 Å
Structure data

PDB-5hms:
X-ray structure of human recombinant 5-aminolaevulinic acid dehydratase (hrALAD).
Method: X-RAY DIFFRACTION / Resolution: 2.8 Å

PDB-5hnr:
The X-ray structure of octameric human native 5-aminolaevulinic acid dehydratase.
Method: X-RAY DIFFRACTION / Resolution: 2.83 Å

PDB-5lzl:
Pyrobaculum calidifontis 5-aminolaevulinic acid dehydratase
Method: X-RAY DIFFRACTION / Resolution: 3.47 Å

PDB-5mhb:
Product-Complex of E.coli 5-Amino Laevulinic Acid Dehydratase
Method: X-RAY DIFFRACTION / Resolution: 2.1 Å

Chemicals

ChemComp-ZN:
Unknown entry

ChemComp-HOH:
WATER

ChemComp-SO4:
SULFATE ION

ChemComp-DAV:
DELTA-AMINO VALERIC ACID

ChemComp-PBG:
3-[5-(AMINOMETHYL)-4-(CARBOXYMETHYL)-1H-PYRROL-3-YL]PROPANOIC ACID

ChemComp-GOL:
GLYCEROL

Source
  • homo sapiens (human)
  • pyrobaculum calidifontis (strain jcm 11548 / va1) (archaea)
  • escherichia coli (E. coli)
KeywordsLYASE / TIM barrel / tetrapyrrole biosynthesis / dehydratase / Tetrapyrrole biosynthesis enzyme / substrate complex. / TIM-barrel

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