1QF6
STRUCTURE OF E. COLI THREONYL-TRNA SYNTHETASE COMPLEXED WITH ITS COGNATE TRNA
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0000049 | molecular_function | tRNA binding |
| A | 0000166 | molecular_function | nucleotide binding |
| A | 0000900 | molecular_function | mRNA regulatory element binding translation repressor activity |
| A | 0002161 | molecular_function | aminoacyl-tRNA deacylase activity |
| A | 0003723 | molecular_function | RNA binding |
| A | 0004812 | molecular_function | aminoacyl-tRNA ligase activity |
| A | 0004829 | molecular_function | threonine-tRNA ligase activity |
| A | 0005515 | molecular_function | protein binding |
| A | 0005524 | molecular_function | ATP binding |
| A | 0005737 | cellular_component | cytoplasm |
| A | 0005829 | cellular_component | cytosol |
| A | 0006412 | biological_process | translation |
| A | 0006417 | biological_process | regulation of translation |
| A | 0006418 | biological_process | tRNA aminoacylation for protein translation |
| A | 0006435 | biological_process | threonyl-tRNA aminoacylation |
| A | 0008270 | molecular_function | zinc ion binding |
| A | 0016874 | molecular_function | ligase activity |
| A | 0042803 | molecular_function | protein homodimerization activity |
| A | 0043039 | biological_process | tRNA aminoacylation |
| A | 0045947 | biological_process | negative regulation of translational initiation |
| A | 0046677 | biological_process | response to antibiotic |
| A | 0046872 | molecular_function | metal ion binding |
| A | 0048027 | molecular_function | mRNA 5'-UTR binding |
| A | 0106074 | biological_process | aminoacyl-tRNA metabolism involved in translational fidelity |
| A | 0140101 | molecular_function | catalytic activity, acting on a tRNA |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE ZN A 1001 |
| Chain | Residue |
| A | CYS334 |
| A | HIS385 |
| A | HIS511 |
| A | HOH1123 |
| site_id | AC2 |
| Number of Residues | 15 |
| Details | BINDING SITE FOR RESIDUE AMP A 1002 |
| Chain | Residue |
| A | PHE379 |
| A | GLN381 |
| A | GLN479 |
| A | CYS480 |
| A | THR482 |
| A | GLY516 |
| A | SER517 |
| A | ARG520 |
| A | HOH1118 |
| B | A76 |
| A | ARG363 |
| A | GLU365 |
| A | MET374 |
| A | ARG375 |
| A | VAL376 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 239 |
| Details | Region: {"description":"N-terminal region which includes the editing domain, important for catalytic efficiency, its loss increases mischarging with L-serine, deacylation of incorrectly charged tRNA no longer occurs, partially complements a deletion strain","evidences":[{"source":"PubMed","id":"10319817","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI2 |
| Number of Residues | 161 |
| Details | Region: {"description":"N2 domain, the editing domain","evidences":[{"source":"PubMed","id":"10319817","evidenceCode":"ECO:0000305"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI3 |
| Number of Residues | 19 |
| Details | Region: {"description":"tRNA acceptor stem binding","evidences":[{"source":"PubMed","id":"10319817","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI4 |
| Number of Residues | 291 |
| Details | Region: {"description":"Catalytic","evidences":[{"source":"HAMAP-Rule","id":"MF_00184","evidenceCode":"ECO:0000255"},{"source":"PubMed","id":"10319817","evidenceCode":"ECO:0000305"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI5 |
| Number of Residues | 107 |
| Details | Region: {"description":"Anticodon recognition","evidences":[{"source":"PubMed","id":"10319817","evidenceCode":"ECO:0000305"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI6 |
| Number of Residues | 36 |
| Details | Binding site: {"evidences":[{"source":"PubMed","id":"11953757","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI7 |
| Number of Residues | 7 |
| Details | Binding site: {"evidences":[{"source":"PubMed","id":"10319817","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"1QF6","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI8 |
| Number of Residues | 29 |
| Details | Binding site: {"evidences":[{"source":"PubMed","id":"10319817","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI9 |
| Number of Residues | 2 |
| Details | Binding site: {"evidences":[{"source":"HAMAP-Rule","id":"MF_00184","evidenceCode":"ECO:0000255"},{"source":"PubMed","id":"10319817","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"10881191","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"11136973","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"11953757","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI10 |
| Number of Residues | 1 |
| Details | Binding site: {"evidences":[{"source":"HAMAP-Rule","id":"MF_00184","evidenceCode":"ECO:0000255"},{"source":"PubMed","id":"10319817","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"10881191","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"11136973","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI11 |
| Number of Residues | 1 |
| Details | Modified residue: {"description":"N6-acetyllysine","evidences":[{"source":"HAMAP-Rule","id":"MF_00184","evidenceCode":"ECO:0000255"},{"source":"PubMed","id":"18723842","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
Catalytic Information from CSA
| site_id | CSA1 |
| Number of Residues | 1 |
| Details | a catalytic site defined by CSA, PubMed 10319817 |
| Chain | Residue | Details |
| A | ARG363 |
| site_id | MCSA1 |
| Number of Residues | 7 |
| Details | M-CSA 540 |
| Chain | Residue | Details |
