| ID: | 2.1.1.85 |
|---|---|
| Description: | Protein-histidine N-methyltransferase. |
| Alternative Name: |
Protein methylase IV. |
Click one PDB to see exact 3D structure provided by NGL.
Note: Use your mouse to drag, rotate, and zoom in and out of the structure. Mouse-over to identify atoms and bonds. Mouse controls documentation.| UniProtKB Enzyme Link: | UniProtKB 2.1.1.85 |
| BRENDA Enzyme Link: | BRENDA 2.1.1.85 |
| KEGG Enzyme Link: | KEGG2.1.1.85 |
| BioCyc Enzyme Link: | BioCyc 2.1.1.85 |
| ExPASy Enzyme Link: | ExPASy2.1.1.85 |
| EC2PDB Enzyme Link: | EC2PDB 2.1.1.85 |
| ExplorEnz Enzyme Link: | ExplorEnz 2.1.1.85 |
| PRIAM enzyme-specific profiles Link: | PRIAM 2.1.1.85 |
| IntEnz Enzyme Link: | IntEnz 2.1.1.85 |
| MEDLINE Enzyme Link: | MEDLINE 2.1.1.85 |
| RHEA:19369 | L-histidyl-[protein] + S-adenosyl-L-methionine = H(+) + N(tele)-methyl-L-histidyl-[protein] + S-adenosyl-L-homocysteine |
| RULE(radius=1) | [*:1]-[S+;H0:2](-[*:3])-[CH3;+0:4].[*:5]:[nH;+0:6]:[*:7]>>[*:1]-[S;H0;+0:2]-[*:3].[*:5]:[n;H0;+0:6](:[*:7])-[CH3;+0:4] |
| Reaction | ![]() |
| Core-to-Core | No scaffolds atoms were exchanged as a result of the reaction |
| Title | Authors | Date | PubMed ID |
|---|---|---|---|
| Partial purification and characterisation of S-adenosylmethionine:protein-histidine N-methyltransferase from rabbit skeletal muscle. | Vijayasarathy C, Rao BS | 1987 Jan 20 | 3801515 |