3mcf
Crystal structure of human diphosphoinositol polyphosphate phosphohydrolase 3-alphaCrystal structure of human diphosphoinositol polyphosphate phosphohydrolase 3-alpha
Structural highlights
Function[NUD10_HUMAN] Cleaves a beta-phosphate from the diphosphate groups in PP-InsP5 (diphosphoinositol pentakisphosphate), suggesting that it may play a role in signal transduction. Also able to catalyze the hydrolysis of dinucleoside oligophosphates, with Ap6A and Ap5A being the preferred substrates. The major reaction products are ADP and p4a from Ap6A and ADP and ATP from Ap5A. Also able to hydrolyze 5-phosphoribose 1-diphosphate. Evolutionary Conservation Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf. |
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OCACategories:
- Human
- Large Structures
- Arrowsmith, C H
- Berg, S van der
- Berglund, H
- Bountra, C
- Collins, R
- Edwards, A M
- Flodin, S
- Flores, A
- Graslund, S
- Hammarstrom, M
- Johansson, I
- Karlberg, T
- Kol, S
- Kotenyova, T
- Moche, M
- Nordlund, P
- Nyman, T
- Persson, C
- Structural genomic
- Schuler, H
- Schutz, P
- Siponen, M I
- Thorsell, A G
- Tresaugues, L
- Wahlberg, E
- Weigelt, J
- Welin, M
- Wisniewska, M
- Aps2
- Diphosphoinositol pentakisphosphate
- Dipp3a
- Hydrolase
- Metal-binding
- Nudix
- Nudt10
- Sgc
- Sgc stockholm
- Signal transduction