Human porphobilinogen deaminase R173W mutant crystallized in the ES2 intermediate state

Human porphobilinogen deaminase R173W mutant crystallized in the ES2 intermediate state Descriptor: 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, GLYCEROL, Porphobilinogen deaminase Authors: Kallio, J.P, Bustad, H.J, Martinez, A. Deposit date: 2020-09-04 Release date: 2021-02-17 Last modified: 2024-11-06 Method: X-RAY DIFFRACTION (1.7 Å) Cite: Characterization of porphobilinogen deaminase mutants reveals that arginine-173 is crucial for polypyrrole elongation mechanism. Iscience, 24, 2021