2BH2
Crystal Structure of E. coli 5-methyluridine methyltransferase RumA in complex with ribosomal RNA substrate and S-adenosylhomocysteine.
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0003723 | molecular_function | RNA binding |
| A | 0005506 | molecular_function | iron ion binding |
| A | 0006364 | biological_process | rRNA processing |
| A | 0006396 | biological_process | RNA processing |
| A | 0008168 | molecular_function | methyltransferase activity |
| A | 0008173 | molecular_function | RNA methyltransferase activity |
| A | 0016740 | molecular_function | transferase activity |
| A | 0031167 | biological_process | rRNA methylation |
| A | 0032259 | biological_process | methylation |
| A | 0046872 | molecular_function | metal ion binding |
| A | 0051536 | molecular_function | iron-sulfur cluster binding |
| A | 0051539 | molecular_function | 4 iron, 4 sulfur cluster binding |
| A | 0070041 | molecular_function | rRNA (uridine-C5-)-methyltransferase activity |
| A | 0070475 | biological_process | rRNA base methylation |
| B | 0003723 | molecular_function | RNA binding |
| B | 0005506 | molecular_function | iron ion binding |
| B | 0006364 | biological_process | rRNA processing |
| B | 0006396 | biological_process | RNA processing |
| B | 0008168 | molecular_function | methyltransferase activity |
| B | 0008173 | molecular_function | RNA methyltransferase activity |
| B | 0016740 | molecular_function | transferase activity |
| B | 0031167 | biological_process | rRNA methylation |
| B | 0032259 | biological_process | methylation |
| B | 0046872 | molecular_function | metal ion binding |
| B | 0051536 | molecular_function | iron-sulfur cluster binding |
| B | 0051539 | molecular_function | 4 iron, 4 sulfur cluster binding |
| B | 0070041 | molecular_function | rRNA (uridine-C5-)-methyltransferase activity |
| B | 0070475 | biological_process | rRNA base methylation |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 21 |
| Details | BINDING SITE FOR RESIDUE SAH A 500 |
| Chain | Residue |
| A | PHE263 |
| A | LEU320 |
| A | GLU341 |
| A | ASN342 |
| A | LEU343 |
| A | GLU344 |
| A | ASP363 |
| A | HOH2112 |
| A | HOH2133 |
| A | HOH2134 |
| A | HOH2135 |
| A | GLN265 |
| C | A1937 |
| C | FMU1939 |
| A | PHE294 |
| A | CYS295 |
| A | ASN299 |
| A | PHE300 |
| A | GLU315 |
| A | GLY316 |
| A | VAL317 |
| site_id | AC2 |
| Number of Residues | 9 |
| Details | BINDING SITE FOR RESIDUE SF4 A 501 |
| Chain | Residue |
| A | CYS81 |
| A | CYS87 |
| A | CYS90 |
| A | GLN93 |
| A | GLN161 |
| A | CYS162 |
| A | PRO163 |
| A | ILE164 |
| C | U1940 |
| site_id | AC3 |
| Number of Residues | 20 |
| Details | BINDING SITE FOR RESIDUE SAH B 500 |
| Chain | Residue |
| B | PHE263 |
| B | GLN265 |
| B | PHE294 |
| B | CYS295 |
| B | MET297 |
| B | ASN299 |
| B | GLU315 |
| B | GLY316 |
| B | VAL317 |
| B | LEU320 |
| B | GLU341 |
| B | ASN342 |
| B | LEU343 |
| B | ASP363 |
| B | HOH2088 |
| B | HOH2129 |
| B | HOH2130 |
| B | HOH2131 |
| D | A1937 |
| D | FMU1939 |
| site_id | AC4 |
| Number of Residues | 7 |
| Details | BINDING SITE FOR RESIDUE SF4 B 501 |
| Chain | Residue |
| B | CYS81 |
| B | CYS87 |
| B | CYS90 |
| B | GLN93 |
| B | GLN161 |
| B | CYS162 |
| B | PRO163 |
Functional Information from PROSITE/UniProt
| site_id | PS01230 |
| Number of Residues | 31 |
| Details | TRMA_1 RNA methyltransferase trmA family signature 1. DPARaGaagvmqqiiklepir....IVYvSCNpaT |
| Chain | Residue | Details |
| A | ASP363-THR393 |
| site_id | PS01231 |
| Number of Residues | 11 |
| Details | TRMA_2 RNA methyltransferase trmA family signature 2. LDmFPHTgHLE |
| Chain | Residue | Details |
| A | LEU414-GLU424 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 44 |
| Details | Region: {"description":"Interaction with RNA"} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI2 |
| Number of Residues | 2 |
| Details | Active site: {"description":"Nucleophile","evidences":[{"source":"HAMAP-Rule","id":"MF_01010","evidenceCode":"ECO:0000255"},{"source":"PubMed","id":"15766524","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI3 |
| Number of Residues | 8 |
| Details | Binding site: {"evidences":[{"source":"PubMed","id":"15016356","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"15766524","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI4 |
| Number of Residues | 12 |
| Details | Binding site: {"evidences":[{"source":"PubMed","id":"15766524","evidenceCode":"ECO:0000305"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI5 |
| Number of Residues | 4 |
| Details | Site: {"description":"Interaction with RNA"} |
| Chain | Residue | Details |
