8PND
 
 | | The ES3 intermediate of hydroxymethylbilane synthase R167Q variant | | Descriptor: | 1,2-ETHANEDIOL, 3-[4-(2-hydroxy-2-oxoethyl)-5-[[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]-3-(3-hydroxy-3-oxopropyl)-1~{H}-pyrrol-2-yl]methyl]-1~{H}-pyrrol-3-yl]propanoic acid, GLYCEROL, ... | | Authors: | Saeter, M.C, Bustad, H.J, Laitaoja, M, Janis, J, Martinez, A, Aarsand, A.K, Kallio, J.P. | | Deposit date: | 2023-06-30 | | Release date: | 2023-11-01 | | Last modified: | 2024-02-14 | | Method: | X-RAY DIFFRACTION (1.9 Å) | | Cite: | One ring closer to a closure: the crystal structure of the ES 3 hydroxymethylbilane synthase intermediate.
Febs J., 291, 2024
|
|
7AAJ
 | | Human porphobilinogen deaminase in complex with cofactor | | Descriptor: | 3-[5-{[3-(2-carboxyethyl)-4-(carboxymethyl)-5-methyl-1H-pyrrol-2-yl]methyl}-4-(carboxymethyl)-1H-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: | 2024-01-31 | | Method: | X-RAY DIFFRACTION (1.8 Å) | | Cite: | Characterization of porphobilinogen deaminase mutants reveals that arginine-173 is crucial for polypyrrole elongation mechanism.
Iscience, 24, 2021
|
|
7AAK
 | | 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: | 2024-05-01 | | 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
|
|
