4IWN
Crystal structure of a putative methyltransferase CmoA in complex with a novel SAM derivative
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0002098 | biological_process | tRNA wobble uridine modification |
| A | 0005829 | cellular_component | cytosol |
| A | 0008168 | molecular_function | methyltransferase activity |
| A | 0016740 | molecular_function | transferase activity |
| A | 0016743 | molecular_function | carboxyl- or carbamoyltransferase activity |
| A | 0042803 | molecular_function | protein homodimerization activity |
| A | 1904047 | molecular_function | S-adenosyl-L-methionine binding |
| B | 0002098 | biological_process | tRNA wobble uridine modification |
| B | 0005829 | cellular_component | cytosol |
| B | 0008168 | molecular_function | methyltransferase activity |
| B | 0016740 | molecular_function | transferase activity |
| B | 0016743 | molecular_function | carboxyl- or carbamoyltransferase activity |
| B | 0042803 | molecular_function | protein homodimerization activity |
| B | 1904047 | molecular_function | S-adenosyl-L-methionine binding |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 21 |
| Details | BINDING SITE FOR RESIDUE GEK A 301 |
| Chain | Residue |
| A | PHE28 |
| A | ASP117 |
| A | ILE118 |
| A | ASN132 |
| A | PHE133 |
| A | PHE137 |
| A | LEU138 |
| A | ARG199 |
| A | HOH405 |
| A | HOH408 |
| A | HOH413 |
| A | TYR39 |
| A | HOH462 |
| A | HOH541 |
| A | GLY64 |
| A | SER66 |
| A | ALA69 |
| A | ASP89 |
| A | ASN90 |
| A | SER91 |
| A | GLY116 |
| site_id | AC2 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE MPD A 302 |
| Chain | Residue |
| A | ASN41 |
| B | GLY38 |
| B | PHE233 |
| B | HOH430 |
| site_id | AC3 |
| Number of Residues | 21 |
| Details | BINDING SITE FOR RESIDUE GEK B 301 |
| Chain | Residue |
| B | PHE28 |
| B | TYR39 |
| B | GLY64 |
| B | SER66 |
| B | ALA69 |
| B | ASP89 |
| B | ASN90 |
| B | SER91 |
| B | GLY116 |
| B | ASP117 |
| B | ILE118 |
| B | ARG119 |
| B | ASN132 |
| B | PHE133 |
| B | THR134 |
| B | PHE137 |
| B | ARG199 |
| B | HOH417 |
| B | HOH440 |
| B | HOH442 |
| B | HOH471 |
| site_id | AC4 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE MPD B 302 |
| Chain | Residue |
| A | ASN41 |
| A | PHE184 |
| A | PHE233 |
| B | SER44 |
| B | HOH421 |
| B | HOH461 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 14 |
| Details | Binding site: {"evidences":[{"source":"HAMAP-Rule","id":"MF_01589","evidenceCode":"ECO:0000255"},{"source":"PubMed","id":"23676670","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"23695253","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
