5ZVG
The crystal structure of NSun6 from Pyrococcus horikoshii with SAM
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0000049 | molecular_function | tRNA binding |
| A | 0001510 | biological_process | RNA methylation |
| A | 0003723 | molecular_function | RNA binding |
| A | 0006396 | biological_process | RNA processing |
| A | 0006400 | biological_process | tRNA modification |
| A | 0008168 | molecular_function | methyltransferase activity |
| A | 0008173 | molecular_function | RNA methyltransferase activity |
| A | 0008757 | molecular_function | S-adenosylmethionine-dependent methyltransferase activity |
| A | 0016428 | molecular_function | tRNA (cytidine-5-)-methyltransferase activity |
| A | 0032259 | biological_process | methylation |
| B | 0000049 | molecular_function | tRNA binding |
| B | 0001510 | biological_process | RNA methylation |
| B | 0003723 | molecular_function | RNA binding |
| B | 0006396 | biological_process | RNA processing |
| B | 0006400 | biological_process | tRNA modification |
| B | 0008168 | molecular_function | methyltransferase activity |
| B | 0008173 | molecular_function | RNA methyltransferase activity |
| B | 0008757 | molecular_function | S-adenosylmethionine-dependent methyltransferase activity |
| B | 0016428 | molecular_function | tRNA (cytidine-5-)-methyltransferase activity |
| B | 0032259 | biological_process | methylation |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 16 |
| Details | binding site for residue SAM B 401 |
| Chain | Residue |
| B | ALA209 |
| B | ARG238 |
| B | MET259 |
| B | ASP260 |
| B | ALA261 |
| B | ASP277 |
| B | TYR304 |
| B | PHE308 |
| B | ALA210 |
| B | ALA211 |
| B | PRO212 |
| B | GLY213 |
| B | GLY214 |
| B | LYS215 |
| B | ASP233 |
| B | LYS234 |
| site_id | AC2 |
| Number of Residues | 16 |
| Details | binding site for residue SAM A 401 |
| Chain | Residue |
| A | ALA209 |
| A | ALA210 |
| A | ALA211 |
| A | PRO212 |
| A | GLY213 |
| A | GLY214 |
| A | LYS215 |
| A | ASP233 |
| A | LYS234 |
| A | ARG238 |
| A | MET259 |
| A | ASP260 |
| A | ALA261 |
| A | ASP277 |
| A | TYR304 |
| A | PHE308 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 2 |
| Details | ACT_SITE: Nucleophile => ECO:0000255|PROSITE-ProRule:PRU01023 |
| Chain | Residue | Details |
| B | CYS327 | |
| A | CYS327 |
| site_id | SWS_FT_FI2 |
| Number of Residues | 8 |
| Details | BINDING: BINDING => ECO:0000255|PROSITE-ProRule:PRU01023, ECO:0000269|PubMed:30541086 |
| Chain | Residue | Details |
| B | ALA209 | |
| B | ASP233 | |
| B | ASP260 | |
| B | ASP277 | |
| A | ALA209 | |
| A | ASP233 | |
| A | ASP260 | |
| A | ASP277 |
| site_id | SWS_FT_FI3 |
| Number of Residues | 4 |
| Details | BINDING: BINDING => ECO:0000269|PubMed:30541086 |
| Chain | Residue | Details |
| B | ARG238 | |
| B | TYR304 | |
| A | ARG238 | |
| A | TYR304 |
