5ZVE
The crystal structure of NSun6 from Pyrococcus horikoshii with SAH
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 | 0016740 | molecular_function | transferase 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 | 0016740 | molecular_function | transferase activity |
B | 0032259 | biological_process | methylation |
Functional Information from PDB Data
site_id | AC1 |
Number of Residues | 18 |
Details | binding site for residue SAH B 401 |
Chain | Residue |
B | ALA209 |
B | ARG238 |
B | MET259 |
B | ASP260 |
B | ALA261 |
B | ASP277 |
B | TYR304 |
B | PHE308 |
B | HOH516 |
B | HOH592 |
B | ALA210 |
B | ALA211 |
B | PRO212 |
B | GLY213 |
B | GLY214 |
B | LYS215 |
B | ASP233 |
B | LYS234 |
site_id | AC2 |
Number of Residues | 17 |
Details | binding site for residue SAH 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 |
A | HOH544 |
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 |