7AAK
Human porphobilinogen deaminase R173W mutant crystallized in the ES2 intermediate state
Summary for 7AAK
Entry DOI | 10.2210/pdb7aak/pdb |
Related | 7AAJ |
Descriptor | Porphobilinogen deaminase, 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, ... (4 entities in total) |
Functional Keywords | pbg-d, hydroxymethylbilane synthase, hmbs, porphobilinogen deaminase, heme biosynthesis, porphyria, acute intermittent porphyria, es2, reaction intermediate, transferase |
Biological source | Homo sapiens (Human) |
Total number of polymer chains | 2 |
Total formula weight | 81158.31 |
Authors | Kallio, J.P.,Bustad, H.J.,Martinez, A. (deposition date: 2020-09-04, release date: 2021-02-17, Last modification date: 2024-05-01) |
Primary citation | Bustad, H.J.,Kallio, J.P.,Laitaoja, M.,Toska, K.,Kursula, I.,Martinez, A.,Janis, J. Characterization of porphobilinogen deaminase mutants reveals that arginine-173 is crucial for polypyrrole elongation mechanism. Iscience, 24:102152-102152, 2021 Cited by PubMed: 33665570DOI: 10.1016/j.isci.2021.102152 PDB entries with the same primary citation |
Experimental method | X-RAY DIFFRACTION (1.7 Å) |
Structure validation
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