EC Number   |
Reference |
|---|
   2.1.1.244 | analysis of crystal structures of NRMT1 and NRMT2 (PDB IDs 2EX4 and 5UBB, determined to 1.75 and 2.0 A, respectively), homology modeling |
758296 |
| 2.1.1.244 | crystal structure with PDB IDs 5WCJ |
756463 |
| 2.1.1.244 | crystal structures with PDB IDs 2EX4, 5E1B, 5E1M, 5E1O, 5E1D, 5E2B, 5E2A, 5CVD, and 5CVE |
756463 |
| 2.1.1.244 | crystal structures with PDB IDs 3CJT, 3CJS, and 3CJR |
756463 |
| 2.1.1.244 | crystal structures with PDB IDs 3EGV, 2NXC, and 2NXN |
756463 |
| 2.1.1.244 | purified recombinant His-tagged enzyme in complex with inhibitor NAM-C3-PKRIA-NH2 , hanging drop vapor diffusion method, mixing of 30 mg/ml protein and 2 mM ligand, with 1.5 M lithium sulfate and 0.1 M Na-HEPES, pH 7.5, 20°C, X-ray diffraction structure determination and analysis at 1.47 A resolution, molecular replacement using the structure PDB ID 6DTN as template, and modelling |
757405 |
| 2.1.1.244 | purified recombinant NRMT1 bound to CENP-A peptide and to the fruit fly H2B peptide in presence of S-adenosyl-L-homocysteine, vapor diffusion method, X-ray diffraction structure determination and analysis at 1.3 A and 1.5 A resolution, respectively |
756877 |
| 2.1.1.244 | recombinant purified full-length wild-type NTMT1 in complex with S-adenosyl-L-homocysteine and a peptide derived from either human (SPKRIA) or mouse (PPKRIA) RCC1, or crystals of NTMT1 in complex with S-adenosyl-L-homocysteine and either the RPK or YPK substrate peptide, sitting drop vapor diffusion method, mixing of 0.001 ml of 37 mg/ml protein and ligand in 20 mM Tris-HCl, pH 7.5, 150 mM NaCl, and 0.5 mM TECP, with 0.001 ml of reservoir solution containing 23-28% PET 3350 and 14-18% Tacsimate, pH 6.0, X-ray diffraction structure determination and analysis, molecular replacement |
736186 |
