Functional Information from GO Data
| Chain | GOid | namespace | contents |
| B | 0002949 | biological_process | tRNA threonylcarbamoyladenosine modification |
| B | 0005737 | cellular_component | cytoplasm |
| B | 0005829 | cellular_component | cytosol |
| B | 0008033 | biological_process | tRNA processing |
| D | 0002949 | biological_process | tRNA threonylcarbamoyladenosine modification |
| D | 0005506 | molecular_function | iron ion binding |
| D | 0005737 | cellular_component | cytoplasm |
| D | 0008033 | biological_process | tRNA processing |
| D | 0016740 | molecular_function | transferase activity |
| D | 0016746 | molecular_function | acyltransferase activity |
| D | 0016747 | molecular_function | acyltransferase activity, transferring groups other than amino-acyl groups |
| D | 0046872 | molecular_function | metal ion binding |
| D | 0061711 | molecular_function | tRNA N(6)-L-threonylcarbamoyladenine synthase activity |
| E | 0000166 | molecular_function | nucleotide binding |
| E | 0002949 | biological_process | tRNA threonylcarbamoyladenosine modification |
| E | 0005524 | molecular_function | ATP binding |
| E | 0005737 | cellular_component | cytoplasm |
| E | 0008033 | biological_process | tRNA processing |
| E | 0046872 | molecular_function | metal ion binding |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 3 |
| Details | binding site for residue PGE B 301 |
| Chain | Residue |
| B | ASP46 |
| B | GLU47 |
| B | HOH418 |
| site_id | AC2 |
| Number of Residues | 2 |
| Details | binding site for residue AE3 B 302 |
| Chain | Residue |
| B | LYS31 |
| B | HOH425 |
| site_id | AC3 |
| Number of Residues | 16 |
| Details | binding site for residue KG4 D 401 |
| Chain | Residue |
| D | PHE164 |
| D | ASP165 |
| D | GLY178 |
| D | PRO179 |
| D | ASP182 |
| D | GLY264 |
| D | VAL265 |
| D | ASN268 |
| D | THR295 |
| D | HOH531 |
| D | HOH538 |
| E | PHE64 |
| D | SER134 |
| D | GLY135 |
| D | GLY136 |
| D | GLY161 |
| site_id | AC4 |
| Number of Residues | 6 |
| Details | binding site for residue ZN D 402 |
| Chain | Residue |
| D | HIS109 |
| D | HIS113 |
| D | HIS137 |
| D | ASP296 |
| D | HOH503 |
| D | HOH535 |
| site_id | AC5 |
| Number of Residues | 5 |
| Details | binding site for residue ADP D 403 |
| Chain | Residue |
| D | PHE248 |
| D | ARG252 |
| D | TRP282 |
| D | TYR284 |
| E | HOH323 |
| site_id | AC6 |
| Number of Residues | 25 |
| Details | binding site for residue ATP E 201 |
| Chain | Residue |
| D | LYS166 |
| D | GLY211 |
| D | LYS213 |
| D | THR214 |
| E | LEU9 |
| E | THR10 |
| E | GLU11 |
| E | LEU14 |
| E | LEU37 |
| E | GLY38 |
| E | ALA39 |
| E | GLY40 |
| E | LYS41 |
| E | THR42 |
| E | THR43 |
| E | GLU108 |
| E | TRP109 |
| E | SER132 |
| E | HIS133 |
| E | ARG134 |
| E | MG202 |
| E | HOH302 |
| E | HOH303 |
| E | HOH308 |
| E | HOH320 |
| site_id | AC7 |
| Number of Residues | 5 |
| Details | binding site for residue MG E 202 |
| Chain | Residue |
| E | THR42 |
| E | GLU108 |
| E | ATP201 |
| E | HOH304 |
| E | HOH308 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 11 |
| Details | Binding site: {"evidences":[{"source":"HAMAP-Rule","id":"MF_01445","evidenceCode":"ECO:0000255"}]} |
6N9A
