6SPN
Structure of the Escherichia coli methionyl-tRNA synthetase complexed with beta-methionine
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0000166 | molecular_function | nucleotide binding |
| A | 0004812 | molecular_function | aminoacyl-tRNA ligase activity |
| A | 0004825 | molecular_function | methionine-tRNA ligase activity |
| A | 0005524 | molecular_function | ATP binding |
| A | 0006418 | biological_process | tRNA aminoacylation for protein translation |
| A | 0006431 | biological_process | methionyl-tRNA aminoacylation |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 4 |
| Details | binding site for residue ZN A 601 |
| Chain | Residue |
| A | CYS145 |
| A | CYS148 |
| A | CYS158 |
| A | CYS161 |
| site_id | AC2 |
| Number of Residues | 8 |
| Details | binding site for residue CIT A 602 |
| Chain | Residue |
| A | HOH940 |
| A | HOH1109 |
| A | HOH1177 |
| A | GLN63 |
| A | LYS132 |
| A | HOH738 |
| A | HOH745 |
| A | HOH797 |
| site_id | AC3 |
| Number of Residues | 14 |
| Details | binding site for residue B3M A 603 |
| Chain | Residue |
| A | LEU13 |
| A | TYR15 |
| A | ASP52 |
| A | TRP253 |
| A | ALA256 |
| A | PRO257 |
| A | TYR260 |
| A | HIS301 |
| A | HOH706 |
| A | HOH840 |
| A | HOH1070 |
| A | HOH1174 |
| A | HOH1290 |
| A | HOH1380 |
| site_id | AC4 |
| Number of Residues | 5 |
| Details | binding site for residue B3M A 604 |
| Chain | Residue |
| A | LYS217 |
| A | LYS295 |
| A | ASP296 |
| A | TYR325 |
| A | ILE367 |
| site_id | AC5 |
| Number of Residues | 6 |
| Details | binding site for residue GOL A 605 |
| Chain | Residue |
| A | GLN458 |
| A | ARG469 |
| A | ASP472 |
| A | HOH714 |
| A | HOH749 |
| A | HOH929 |
Functional Information from PROSITE/UniProt
| site_id | PS00178 |
| Number of Residues | 12 |
| Details | AA_TRNA_LIGASE_I Aminoacyl-transfer RNA synthetases class-I signature. PyaNGsIHLGHM |
| Chain | Residue | Details |
| A | PRO14-MET25 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 10 |
| Details | Motif: {"description":"'HIGH' region","evidences":[{"evidenceCode":"ECO:0000305"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI2 |
| Number of Residues | 4 |
| Details | Motif: {"description":"'KMSKS' region","evidences":[{"source":"PubMed","id":"7932711","evidenceCode":"ECO:0000305"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI3 |
| Number of Residues | 2 |
| Details | Binding site: {"evidences":[{"source":"PubMed","id":"11243794","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"12946347","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"1F4L","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"1PG2","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI4 |
| Number of Residues | 4 |
| Details | Binding site: {"evidences":[{"source":"PubMed","id":"10600385","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"11243794","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"12946347","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"8515465","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"8515466","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"1F4L","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"1MEA","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"1MED","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"1P7P","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"1PFU","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"1PFV","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"1PFW","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"1PFY","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"1QQT","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI5 |
| Number of Residues | 1 |
| Details | Binding site: {"evidences":[{"source":"PubMed","id":"2254937","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
