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-Structure paper
Title | Characterization of porphobilinogen deaminase mutants reveals that arginine-173 is crucial for polypyrrole elongation mechanism. |
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Journal, issue, pages | Iscience, Vol. 24, Page 102152-102152, Year 2021 |
Publish date | Sep 4, 2020 (structure data deposition date) |
![]() | Bustad, H.J. / Kallio, J.P. / Laitaoja, M. / Toska, K. / Kursula, I. / Martinez, A. / Janis, J. |
![]() | ![]() ![]() |
Methods | X-ray diffraction |
Resolution | 1.7 - 1.8 Å |
Structure data | ![]() PDB-7aaj: ![]() PDB-7aak: |
Chemicals | ![]() ChemComp-DPM: ![]() ChemComp-GOL: ![]() ChemComp-HOH: ![]() ChemComp-7J8: |
Source |
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![]() | TRANSFERASE / PBG-D / Hydroxymethylbilane synthase / HMBS / Porphobilinogen deaminase / heme biosynthesis / porphyria / acute intermittent porphyria / ES2 / reaction intermediate |