1EVL
CRYSTAL STRUCTURE OF A TRUNCATED FORM OF THREONYL-TRNA SYNTHETASE WITH A THREONYL 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 |
| C | 0000166 | molecular_function | nucleotide binding |
| C | 0004812 | molecular_function | aminoacyl-tRNA ligase activity |
| C | 0004829 | molecular_function | threonine-tRNA ligase activity |
| C | 0005524 | molecular_function | ATP binding |
| C | 0005737 | cellular_component | cytoplasm |
| C | 0006418 | biological_process | tRNA aminoacylation for protein translation |
| C | 0006435 | biological_process | threonyl-tRNA aminoacylation |
| D | 0000166 | molecular_function | nucleotide binding |
| D | 0004812 | molecular_function | aminoacyl-tRNA ligase activity |
| D | 0004829 | molecular_function | threonine-tRNA ligase activity |
| D | 0005524 | molecular_function | ATP binding |
| D | 0005737 | cellular_component | cytoplasm |
| D | 0006418 | biological_process | tRNA aminoacylation for protein translation |
| D | 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 1 |
| Chain | Residue |
| A | CYS334 |
| A | HIS385 |
| A | HIS511 |
| A | TSB2002 |
| site_id | AC2 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE ZN B 1 |
| Chain | Residue |
| B | CYS334 |
| B | HIS385 |
| B | HIS511 |
| B | TSB3002 |
| site_id | AC3 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE ZN C 1 |
| Chain | Residue |
| C | HIS385 |
| C | HIS511 |
| C | TSB4002 |
| C | CYS334 |
| site_id | AC4 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE ZN D 1 |
| Chain | Residue |
| D | CYS334 |
| D | HIS385 |
| D | HIS511 |
| D | TSB5002 |
| site_id | AC5 |
| Number of Residues | 23 |
| Details | BINDING SITE FOR RESIDUE TSB A 2002 |
| Chain | Residue |
| A | ZN1 |
| A | MET332 |
| 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 | THR482 |
| A | GLN484 |
| A | HIS511 |
| A | GLY516 |
| A | SER517 |
| A | ARG520 |
| A | HOH2039 |
| A | HOH2192 |
| site_id | AC6 |
| Number of Residues | 23 |
| Details | BINDING SITE FOR RESIDUE TSB B 3002 |
| Chain | Residue |
| B | ZN1 |
| 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 | HOH3003 |
| B | HOH3055 |
| B | HOH3097 |
| site_id | AC7 |
| Number of Residues | 22 |
| Details | BINDING SITE FOR RESIDUE TSB C 4002 |
| Chain | Residue |
| C | ZN1 |
| C | MET332 |
| C | CYS334 |
| C | ARG363 |
| C | GLU365 |
| C | MET374 |
| C | ARG375 |
| C | VAL376 |
| C | PHE379 |
| C | GLN381 |
| C | ASP383 |
| C | HIS385 |
| C | TYR462 |
| C | GLN479 |
| C | CYS480 |
| C | GLN484 |
| C | HIS511 |
| C | GLY516 |
| C | SER517 |
| C | ARG520 |
| C | HOH4068 |
| C | HOH4142 |
| site_id | AC8 |
| Number of Residues | 24 |
| Details | BINDING SITE FOR RESIDUE TSB D 5002 |
| Chain | Residue |
| D | CYS480 |
| D | THR482 |
| D | GLN484 |
| D | HIS511 |
| D | GLY516 |
| D | SER517 |
| D | ARG520 |
| D | HOH5035 |
| D | HOH5315 |
| D | ZN1 |
| D | MET332 |
| D | CYS334 |
| D | ARG363 |
| D | GLU365 |
| D | MET374 |
| D | ARG375 |
| D | VAL376 |
| D | PHE379 |
| D | GLN381 |
| D | ASP383 |
| D | HIS385 |
| D | TYR462 |
| D | LYS465 |
| D | GLN479 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 16 |
| Details | BINDING: BINDING => ECO:0000269|PubMed:11953757 |
| Chain | Residue | Details |
| A | LYS246 | |
| C | ASN342 | |
| C | LEU489 | |
| C | ASP615 | |
| D | LYS246 | |
| D | ASN342 | |
| D | LEU489 | |
| D | ASP615 | |
| A | ASN342 | |
| A | LEU489 | |
| A | ASP615 | |
| B | LYS246 | |
| B | ASN342 | |
| B | LEU489 | |
| B | ASP615 | |
| C | LYS246 |
| site_id | SWS_FT_FI2 |
| Number of Residues | 20 |
| Details | BINDING: BINDING => ECO:0000269|PubMed:10319817, ECO:0007744|PDB:1QF6 |
| Chain | Residue | Details |
| A | HIS309 | |
| B | SER517 | |
| C | HIS309 | |
| C | VAL376 | |
| C | GLN381 | |
| C | GLN479 | |
| C | SER517 | |
| D | HIS309 | |
| D | VAL376 | |
| D | GLN381 | |
| D | GLN479 | |
| A | VAL376 | |
| D | SER517 | |
| A | GLN381 | |
| A | GLN479 | |
| A | SER517 | |
| B | HIS309 | |
| B | VAL376 | |
| B | GLN381 | |
| B | GLN479 |
| site_id | SWS_FT_FI3 |
| Number of Residues | 56 |
| Details | BINDING: BINDING => ECO:0000269|PubMed:10319817 |
| Chain | Residue | Details |
| A | TYR313 | |
| A | ILE547 | |
| A | ASN575 | |
| A | ARG589 | |
| A | VAL595 | |
| A | ARG609 | |
| B | TYR313 | |
| B | ARG325 | |
| B | TYR348 | |
| B | ARG363 | |
| B | ARG375 | |
| A | ARG325 | |
| B | PHE379 | |
| B | TYR462 | |
| B | GLN484 | |
| B | ARG520 | |
| B | ILE547 | |
| B | ASN575 | |
| B | ARG589 | |
| B | VAL595 | |
| B | ARG609 | |
| C | TYR313 | |
| A | TYR348 | |
| C | ARG325 | |
| C | TYR348 | |
| C | ARG363 | |
| C | ARG375 | |
| C | PHE379 | |
| C | TYR462 | |
| C | GLN484 | |
| C | ARG520 | |
| C | ILE547 | |
| C | ASN575 | |
| A | ARG363 | |
| C | ARG589 | |
| C | VAL595 | |
| C | ARG609 | |
| D | TYR313 | |
| D | ARG325 | |
| D | TYR348 | |
| D | ARG363 | |
| D | ARG375 | |
| D | PHE379 | |
| D | TYR462 | |
| A | ARG375 | |
| D | GLN484 | |
| D | ARG520 | |
| D | ILE547 | |
| D | ASN575 | |
| D | ARG589 | |
| D | VAL595 | |
| D | ARG609 | |
| A | PHE379 | |
| A | TYR462 | |
| A | GLN484 | |
| A | ARG520 |
| site_id | SWS_FT_FI4 |
| Number of Residues | 8 |
| Details | BINDING: BINDING => ECO:0000255|HAMAP-Rule:MF_00184, ECO:0000269|PubMed:10319817, ECO:0000269|PubMed:10881191, ECO:0000269|PubMed:11136973, ECO:0000269|PubMed:11953757 |
| Chain | Residue | Details |
| A | CYS334 | |
| A | HIS385 | |
| B | CYS334 | |
| B | HIS385 | |
| C | CYS334 | |
| C | HIS385 | |
| D | CYS334 | |
| D | HIS385 |
| site_id | SWS_FT_FI5 |
| Number of Residues | 4 |
| Details | BINDING: BINDING => ECO:0000255|HAMAP-Rule:MF_00184, ECO:0000269|PubMed:10319817, ECO:0000269|PubMed:10881191, ECO:0000269|PubMed:11136973 |
| Chain | Residue | Details |
| A | HIS511 | |
| B | HIS511 | |
| C | HIS511 | |
| D | HIS511 |
| site_id | SWS_FT_FI6 |
| Number of Residues | 4 |
| Details | MOD_RES: N6-acetyllysine => ECO:0000255|HAMAP-Rule:MF_00184, ECO:0000269|PubMed:18723842 |
| Chain | Residue | Details |
| A | LYS286 | |
| B | LYS286 | |
| C | LYS286 | |
| D | LYS286 |
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 | CSA3 |
| Number of Residues | 1 |
| Details | Annotated By Reference To The Literature 1qf6 |
| Chain | Residue | Details |
| C | ARG363 |
| site_id | CSA4 |
| Number of Residues | 1 |
| Details | Annotated By Reference To The Literature 1qf6 |
| Chain | Residue | Details |
| D | 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 |
| site_id | MCSA3 |
| Number of Residues | 7 |
| Details | M-CSA 540 |
| Chain | Residue | Details |
| C | CYS334 | electrostatic stabiliser, metal ligand |
| C | ARG363 | electrostatic stabiliser |
| C | GLN381 | electrostatic stabiliser |
| C | ASP383 | electrostatic stabiliser |
| C | HIS385 | metal ligand |
| C | LYS465 | electrostatic stabiliser |
| C | HIS511 | metal ligand |
| site_id | MCSA4 |
| Number of Residues | 7 |
| Details | M-CSA 540 |
| Chain | Residue | Details |
| D | CYS334 | electrostatic stabiliser, metal ligand |
| D | ARG363 | electrostatic stabiliser |
| D | GLN381 | electrostatic stabiliser |
| D | ASP383 | electrostatic stabiliser |
| D | HIS385 | metal ligand |
| D | LYS465 | electrostatic stabiliser |
| D | HIS511 | metal ligand |
