2QG6
Crystal structure of human nicotinamide riboside kinase (NRK1) in complex with nicotinamide mononucleotide (NMN)
Summary for 2QG6
| Entry DOI | 10.2210/pdb2qg6/pdb |
| Descriptor | Nicotinamide riboside kinase 1, PHOSPHATE ION, BETA-NICOTINAMIDE RIBOSE MONOPHOSPHATE, ... (4 entities in total) |
| Functional Keywords | nrk, nicotinamide riboside kinase, nad+, nucleoside monophosphate (nmp) kinase, nicotinamide mononucleotide, adp, tiazofurin, signaling protein, transferase |
| Biological source | Homo sapiens (human) |
| Total number of polymer chains | 1 |
| Total formula weight | 23974.85 |
| Authors | Khan, J.A.,Xiang, S.,Tong, L. (deposition date: 2007-06-28, release date: 2007-10-02, Last modification date: 2017-10-18) |
| Primary citation | Khan, J.A.,Xiang, S.,Tong, L. Crystal structure of human nicotinamide riboside kinase Structure, 15:1005-1013, 2007 Cited by PubMed Abstract: Nicotinamide riboside kinase (NRK) has an important role in the biosynthesis of NAD(+) as well as the activation of tiazofurin and other NR analogs for anticancer therapy. NRK belongs to the deoxynucleoside kinase and nucleoside monophosphate (NMP) kinase superfamily, although the degree of sequence conservation is very low. We report here the crystal structures of human NRK1 in a binary complex with the reaction product nicotinamide mononucleotide (NMN) at 1.5 A resolution and in a ternary complex with ADP and tiazofurin at 2.7 A resolution. The active site is located in a groove between the central parallel beta sheet core and the LID and NMP-binding domains. The hydroxyl groups on the ribose of NR are recognized by Asp56 and Arg129, and Asp36 is the general base of the enzyme. Mutation of residues in the active site can abolish the catalytic activity of the enzyme, confirming the structural observations. PubMed: 17698003DOI: 10.1016/j.str.2007.06.017 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (1.5 Å) |
Structure validation
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