1FYF
CRYSTAL STRUCTURE OF A TRUNCATED FORM OF THREONYL-TRNA SYNTHETASE COMPLEXED WITH A SERYL ADENYLATE ANALOG
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0000166 | molecular_function | nucleotide binding |
| A | 0004812 | molecular_function | aminoacyl-tRNA ligase activity |
| A | 0004829 | molecular_function | threonine-tRNA ligase activity |
| A | 0005524 | molecular_function | ATP binding |
| A | 0005737 | cellular_component | cytoplasm |
| A | 0006418 | biological_process | tRNA aminoacylation for protein translation |
| A | 0006435 | biological_process | threonyl-tRNA aminoacylation |
| B | 0000166 | molecular_function | nucleotide binding |
| B | 0004812 | molecular_function | aminoacyl-tRNA ligase activity |
| B | 0004829 | molecular_function | threonine-tRNA ligase activity |
| B | 0005524 | molecular_function | ATP binding |
| B | 0005737 | cellular_component | cytoplasm |
| B | 0006418 | biological_process | tRNA aminoacylation for protein translation |
| B | 0006435 | biological_process | threonyl-tRNA aminoacylation |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE ZN A 650 |
| Chain | Residue |
| A | CYS334 |
| A | HIS385 |
| A | HIS511 |
| A | SSA1001 |
| site_id | AC2 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE ZN B 650 |
| Chain | Residue |
| B | CYS334 |
| B | HIS385 |
| B | HIS511 |
| B | SSA2001 |
| site_id | AC3 |
| Number of Residues | 22 |
| Details | BINDING SITE FOR RESIDUE SSA A 1001 |
| Chain | Residue |
| A | CYS334 |
| A | ARG363 |
| A | GLU365 |
| A | MET374 |
| A | ARG375 |
| A | VAL376 |
| A | PHE379 |
| A | GLN381 |
| A | ASP383 |
| A | HIS385 |
| A | TYR462 |
| A | GLN479 |
| A | CYS480 |
| A | GLN484 |
| A | HIS511 |
| A | GLY516 |
| A | SER517 |
| A | ARG520 |
| A | ZN650 |
| A | HOH1012 |
| A | HOH1071 |
| A | MET332 |
| site_id | AC4 |
| Number of Residues | 22 |
| Details | BINDING SITE FOR RESIDUE SSA B 2001 |
| Chain | Residue |
| B | MET332 |
| B | CYS334 |
| B | ARG363 |
| B | GLU365 |
| B | MET374 |
| B | ARG375 |
| B | VAL376 |
| B | PHE379 |
| B | GLN381 |
| B | ASP383 |
| B | HIS385 |
| B | TYR462 |
| B | GLN479 |
| B | CYS480 |
| B | GLN484 |
| B | HIS511 |
| B | GLY516 |
| B | SER517 |
| B | ARG520 |
| B | ZN650 |
| B | HOH2006 |
| B | HOH2066 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 582 |
| 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_FI2 |
| Number of Residues | 214 |
| Details | Region: {"description":"Anticodon recognition","evidences":[{"source":"PubMed","id":"10319817","evidenceCode":"ECO:0000305"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI3 |
| Number of Residues | 72 |
| Details | Binding site: {"evidences":[{"source":"PubMed","id":"11953757","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI4 |
| Number of Residues | 14 |
| 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_FI5 |
| Number of Residues | 58 |
| Details | Binding site: {"evidences":[{"source":"PubMed","id":"10319817","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI6 |
| Number of Residues | 4 |
| 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_FI7 |
| 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"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI8 |
| Number of Residues | 2 |
| 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 | Annotated By Reference To The Literature 1qf6 |
| Chain | Residue | Details |
| A | ARG363 |
| site_id | CSA2 |
| Number of Residues | 1 |
| Details | Annotated By Reference To The Literature 1qf6 |
| Chain | Residue | Details |
| B | ARG363 |
| site_id | MCSA1 |
| Number of Residues | 7 |
| Details | M-CSA 540 |
| Chain | Residue | Details |
| A | CYS334 | electrostatic stabiliser, metal ligand |
| A | ARG363 | electrostatic stabiliser |
| A | GLN381 | electrostatic stabiliser |
| A | ASP383 | electrostatic stabiliser |
| A | HIS385 | metal ligand |
| A | LYS465 | electrostatic stabiliser |
| A | HIS511 | metal ligand |
| site_id | MCSA2 |
| Number of Residues | 7 |
| Details | M-CSA 540 |
| Chain | Residue | Details |
| B | CYS334 | electrostatic stabiliser, metal ligand |
| B | ARG363 | electrostatic stabiliser |
| B | GLN381 | electrostatic stabiliser |
| B | ASP383 | electrostatic stabiliser |
| B | HIS385 | metal ligand |
| B | LYS465 | electrostatic stabiliser |
| B | HIS511 | metal ligand |
