5E8J
Crystal structure of mRNA cap guanine-N7 methyltransferase in complex with RAM
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0004482 | molecular_function | mRNA 5'-cap (guanine-N7-)-methyltransferase activity |
| A | 0006370 | biological_process | 7-methylguanosine mRNA capping |
| B | 0004482 | molecular_function | mRNA 5'-cap (guanine-N7-)-methyltransferase activity |
| B | 0006370 | biological_process | 7-methylguanosine mRNA capping |
| C | 0003723 | molecular_function | RNA binding |
| C | 0031533 | cellular_component | mRNA capping enzyme complex |
| C | 0106005 | biological_process | RNA 5'-cap (guanine-N7)-methylation |
| D | 0003723 | molecular_function | RNA binding |
| D | 0031533 | cellular_component | mRNA capping enzyme complex |
| D | 0106005 | biological_process | RNA 5'-cap (guanine-N7)-methylation |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 6 |
| Details | binding site for residue GOL A 501 |
| Chain | Residue |
| A | GLY207 |
| A | LYS208 |
| A | GLY209 |
| A | GLY210 |
| A | SAH502 |
| A | HOH633 |
| site_id | AC2 |
| Number of Residues | 18 |
| Details | binding site for residue SAH A 502 |
| Chain | Residue |
| A | GLY207 |
| A | ASP227 |
| A | ILE228 |
| A | ALA260 |
| A | ASP261 |
| A | SER262 |
| A | GLN284 |
| A | PHE285 |
| A | VAL286 |
| A | TYR289 |
| A | MET300 |
| A | GOL501 |
| A | HOH633 |
| A | HOH654 |
| A | HOH663 |
| A | LYS180 |
| A | GLY205 |
| A | CYS206 |
| site_id | AC3 |
| Number of Residues | 14 |
| Details | binding site for residue SAH B 501 |
| Chain | Residue |
| B | LYS180 |
| B | GLY205 |
| B | CYS206 |
| B | GLY207 |
| B | ASP227 |
| B | ILE228 |
| B | ALA260 |
| B | ASP261 |
| B | SER262 |
| B | GLN284 |
| B | PHE285 |
| B | VAL286 |
| B | TYR289 |
| B | HOH650 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 616 |
| Details | Domain: {"description":"mRNA cap 0 methyltransferase","evidences":[{"source":"PROSITE-ProRule","id":"PRU00895","evidenceCode":"ECO:0000255"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI2 |
| Number of Residues | 2 |
| Details | Binding site: {"evidences":[{"source":"PROSITE-ProRule","id":"PRU00895","evidenceCode":"ECO:0000255"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI3 |
| Number of Residues | 6 |
| Details | Binding site: {"evidences":[{"source":"PROSITE-ProRule","id":"PRU00895","evidenceCode":"ECO:0000255"},{"source":"PubMed","id":"27422871","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"3BGV","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"5E9J","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"5E9W","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI4 |
| Number of Residues | 6 |
| Details | Binding site: {"evidences":[{"source":"PubMed","id":"27422871","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"3BGV","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"5E9J","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"5E9W","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI5 |
| Number of Residues | 12 |
| Details | Site: {"description":"mRNA cap binding","evidences":[{"source":"PROSITE-ProRule","id":"PRU00895","evidenceCode":"ECO:0000255"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI6 |
| Number of Residues | 12 |
| Details | Motif: {"description":"RNMT-activating domain","evidences":[{"source":"PubMed","id":"27422871","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI7 |
| Number of Residues | 2 |
| Details | Modified residue: {"description":"Phosphoserine","evidences":[{"source":"PubMed","id":"18220336","evidenceCode":"ECO:0007744"},{"source":"PubMed","id":"18669648","evidenceCode":"ECO:0007744"},{"source":"PubMed","id":"19690332","evidenceCode":"ECO:0007744"},{"source":"PubMed","id":"20068231","evidenceCode":"ECO:0007744"},{"source":"PubMed","id":"23186163","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
