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Structure paper

TitleCharacterization of porphobilinogen deaminase mutants reveals that arginine-173 is crucial for polypyrrole elongation mechanism.
Journal, issue, pagesIscience, Vol. 24, Page 102152-102152, Year 2021
Publish dateSep 4, 2020 (structure data deposition date)
AuthorsBustad, H.J. / Kallio, J.P. / Laitaoja, M. / Toska, K. / Kursula, I. / Martinez, A. / Janis, J.
External linksIscience / PubMed:33665570
MethodsX-ray diffraction
Resolution1.7 - 1.8 Å
Structure data

PDB-7aaj:
Human porphobilinogen deaminase in complex with cofactor
Method: X-RAY DIFFRACTION / Resolution: 1.8 Å

PDB-7aak:
Human porphobilinogen deaminase R173W mutant crystallized in the ES2 intermediate state
Method: X-RAY DIFFRACTION / Resolution: 1.7 Å

Chemicals

ChemComp-DPM:
3-[5-{[3-(2-carboxyethyl)-4-(carboxymethyl)-5-methyl-1H-pyrrol-2-yl]methyl}-4-(carboxymethyl)-1H-pyrrol-3-yl]propanoic acid

ChemComp-GOL:
GLYCEROL

ChemComp-HOH:
WATER

ChemComp-7J8:
3-[4-(2-hydroxy-2-oxoethyl)-5-[[4-(2-hydroxy-2-oxoethyl)-5-[[4-(2-hydroxy-2-oxoethyl)-5-[[4-(2-hydroxy-2-oxoethyl)-3-(3-hydroxy-3-oxopropyl)-5-methyl-1~{H}-pyrrol-2-yl]methyl]-3-(3-hydroxy-3-oxopropyl)-1~{H}-pyrrol-2-yl]methyl]-3-(3-hydroxy-3-oxopropyl)-1~{H}-pyrrol-2-yl]methyl]-1~{H}-pyrrol-3-yl]propanoic acid

Source
  • homo sapiens (human)
KeywordsTRANSFERASE / PBG-D / Hydroxymethylbilane synthase / HMBS / Porphobilinogen deaminase / heme biosynthesis / porphyria / acute intermittent porphyria / ES2 / reaction intermediate

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