1KOG
Crystal structure of E. coli threonyl-tRNA synthetase interacting with the essential domain of its mRNA operator
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 |
E | 0000166 | molecular_function | nucleotide binding |
E | 0004812 | molecular_function | aminoacyl-tRNA ligase activity |
E | 0004829 | molecular_function | threonine-tRNA ligase activity |
E | 0005524 | molecular_function | ATP binding |
E | 0005737 | cellular_component | cytoplasm |
E | 0006418 | biological_process | tRNA aminoacylation for protein translation |
E | 0006435 | biological_process | threonyl-tRNA aminoacylation |
F | 0000166 | molecular_function | nucleotide binding |
F | 0004812 | molecular_function | aminoacyl-tRNA ligase activity |
F | 0004829 | molecular_function | threonine-tRNA ligase activity |
F | 0005524 | molecular_function | ATP binding |
F | 0005737 | cellular_component | cytoplasm |
F | 0006418 | biological_process | tRNA aminoacylation for protein translation |
F | 0006435 | biological_process | threonyl-tRNA aminoacylation |
G | 0000166 | molecular_function | nucleotide binding |
G | 0004812 | molecular_function | aminoacyl-tRNA ligase activity |
G | 0004829 | molecular_function | threonine-tRNA ligase activity |
G | 0005524 | molecular_function | ATP binding |
G | 0005737 | cellular_component | cytoplasm |
G | 0006418 | biological_process | tRNA aminoacylation for protein translation |
G | 0006435 | biological_process | threonyl-tRNA aminoacylation |
H | 0000166 | molecular_function | nucleotide binding |
H | 0004812 | molecular_function | aminoacyl-tRNA ligase activity |
H | 0004829 | molecular_function | threonine-tRNA ligase activity |
H | 0005524 | molecular_function | ATP binding |
H | 0005737 | cellular_component | cytoplasm |
H | 0006418 | biological_process | tRNA aminoacylation for protein translation |
H | 0006435 | biological_process | threonyl-tRNA aminoacylation |
Functional Information from PDB Data
site_id | AC1 |
Number of Residues | 5 |
Details | BINDING SITE FOR RESIDUE ZN A 1 |
Chain | Residue |
A | CYS334 |
A | HIS385 |
A | TYR462 |
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 | 5 |
Details | BINDING SITE FOR RESIDUE ZN C 1 |
Chain | Residue |
C | CYS334 |
C | HIS385 |
C | TYR462 |
C | HIS511 |
C | TSB4002 |
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 | 4 |
Details | BINDING SITE FOR RESIDUE ZN E 1 |
Chain | Residue |
E | CYS334 |
E | HIS385 |
E | HIS511 |
E | TSB6002 |
site_id | AC6 |
Number of Residues | 5 |
Details | BINDING SITE FOR RESIDUE ZN F 1 |
Chain | Residue |
F | CYS334 |
F | HIS385 |
F | TYR462 |
F | HIS511 |
F | TSB7002 |
site_id | AC7 |
Number of Residues | 5 |
Details | BINDING SITE FOR RESIDUE ZN G 1 |
Chain | Residue |
G | CYS334 |
G | HIS385 |
G | TYR462 |
G | HIS511 |
G | TSB8002 |
site_id | AC8 |
Number of Residues | 5 |
Details | BINDING SITE FOR RESIDUE ZN H 1 |
Chain | Residue |
H | CYS334 |
H | HIS385 |
H | TYR462 |
H | HIS511 |
H | TSB9002 |
site_id | AC9 |
Number of Residues | 22 |
Details | BINDING SITE FOR RESIDUE TSB A 2002 |
Chain | Residue |
A | ZN1 |
A | MET332 |
A | CYS334 |
A | ARG363 |
A | GLU365 |
A | MET374 |
A | VAL376 |
A | PHE379 |
A | GLN381 |
A | ASP383 |
A | ALA384 |
A | HIS385 |
A | TYR462 |
A | GLN479 |
A | CYS480 |
A | THR482 |
A | GLN484 |
A | HIS511 |
A | ARG512 |
A | GLY516 |
A | SER517 |
A | ARG520 |
site_id | BC1 |
Number of Residues | 22 |
Details | BINDING SITE FOR RESIDUE TSB B 3002 |
Chain | Residue |
B | ZN1 |
B | MET332 |
B | CYS334 |
B | ARG363 |
B | GLU365 |
B | MET374 |
B | VAL376 |
B | PHE379 |
B | GLN381 |
B | ASP383 |
B | ALA384 |
B | HIS385 |
B | TYR462 |
B | GLN479 |
B | CYS480 |
B | THR482 |
B | GLN484 |
B | HIS511 |
B | ARG512 |
B | GLY516 |
B | SER517 |
B | ARG520 |
site_id | BC2 |
Number of Residues | 21 |
Details | BINDING SITE FOR RESIDUE TSB C 4002 |
Chain | Residue |
C | GLY516 |
C | SER517 |
C | ARG520 |
C | ZN1 |
C | MET332 |
C | CYS334 |
C | ARG363 |
C | GLU365 |
C | MET374 |
C | VAL376 |
C | PHE379 |
C | GLN381 |
C | ASP383 |
C | ALA384 |
C | HIS385 |
C | TYR462 |
C | GLN479 |
C | CYS480 |
C | GLN484 |
C | HIS511 |
C | ARG512 |
site_id | BC3 |
Number of Residues | 22 |
Details | BINDING SITE FOR RESIDUE TSB D 5002 |
Chain | Residue |
D | ZN1 |
D | MET332 |
D | CYS334 |
D | ARG363 |
D | GLU365 |
D | MET374 |
D | VAL376 |
D | PHE379 |
D | GLN381 |
D | ASP383 |
D | ALA384 |
D | HIS385 |
D | TYR462 |
D | GLN479 |
D | CYS480 |
D | THR482 |
D | GLN484 |
D | HIS511 |
D | ARG512 |
D | GLY516 |
D | SER517 |
D | ARG520 |
site_id | BC4 |
Number of Residues | 23 |
Details | BINDING SITE FOR RESIDUE TSB E 6002 |
Chain | Residue |
E | ZN1 |
E | MET332 |
E | CYS334 |
E | ARG363 |
E | GLU365 |
E | MET374 |
E | VAL376 |
E | PHE379 |
E | GLN381 |
E | ASP383 |
E | ALA384 |
E | HIS385 |
E | TYR462 |
E | GLN479 |
E | CYS480 |
E | THR482 |
E | GLN484 |
E | HIS511 |
E | ARG512 |
E | ALA513 |
E | GLY516 |
E | SER517 |
E | ARG520 |
site_id | BC5 |
Number of Residues | 22 |
Details | BINDING SITE FOR RESIDUE TSB F 7002 |
Chain | Residue |
F | ZN1 |
F | MET332 |
F | CYS334 |
F | ARG363 |
F | GLU365 |
F | MET374 |
F | VAL376 |
F | PHE379 |
F | GLN381 |
F | ASP383 |
F | ALA384 |
F | HIS385 |
F | TYR462 |
F | GLN479 |
F | CYS480 |
F | THR482 |
F | GLN484 |
F | HIS511 |
F | ARG512 |
F | GLY516 |
F | SER517 |
F | ARG520 |
site_id | BC6 |
Number of Residues | 22 |
Details | BINDING SITE FOR RESIDUE TSB G 8002 |
Chain | Residue |
G | ZN1 |
G | MET332 |
G | CYS334 |
G | ARG363 |
G | GLU365 |
G | MET374 |
G | VAL376 |
G | PHE379 |
G | GLN381 |
G | ASP383 |
G | ALA384 |
G | HIS385 |
G | TYR462 |
G | GLN479 |
G | CYS480 |
G | THR482 |
G | GLN484 |
G | HIS511 |
G | ARG512 |
G | GLY516 |
G | SER517 |
G | ARG520 |
site_id | BC7 |
Number of Residues | 22 |
Details | BINDING SITE FOR RESIDUE TSB H 9002 |
Chain | Residue |
H | ZN1 |
H | MET332 |
H | CYS334 |
H | ARG363 |
H | GLU365 |
H | MET374 |
H | VAL376 |
H | PHE379 |
H | GLN381 |
H | ASP383 |
H | ALA384 |
H | HIS385 |
H | TYR462 |
H | GLN479 |
H | CYS480 |
H | THR482 |
H | GLN484 |
H | HIS511 |
H | ARG512 |
H | GLY516 |
H | SER517 |
H | ARG520 |
Functional Information from SwissProt/UniProt
site_id | SWS_FT_FI1 |
Number of Residues | 32 |
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 | |
E | LYS246 | |
E | ASN342 | |
E | LEU489 | |
A | ASN342 | |
E | ASP615 | |
F | LYS246 | |
F | ASN342 | |
F | LEU489 | |
F | ASP615 | |
G | LYS246 | |
G | ASN342 | |
G | LEU489 | |
G | ASP615 | |
H | LYS246 | |
A | LEU489 | |
H | ASN342 | |
H | LEU489 | |
H | ASP615 | |
A | ASP615 | |
B | LYS246 | |
B | ASN342 | |
B | LEU489 | |
B | ASP615 | |
C | LYS246 |
site_id | SWS_FT_FI2 |
Number of Residues | 40 |
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 | |
E | HIS309 | |
E | VAL376 | |
E | GLN381 | |
E | GLN479 | |
E | SER517 | |
F | HIS309 | |
F | VAL376 | |
F | GLN381 | |
F | GLN479 | |
A | GLN381 | |
F | SER517 | |
G | HIS309 | |
G | VAL376 | |
G | GLN381 | |
G | GLN479 | |
G | SER517 | |
H | HIS309 | |
H | VAL376 | |
H | GLN381 | |
H | GLN479 | |
A | GLN479 | |
H | SER517 | |
A | SER517 | |
B | HIS309 | |
B | VAL376 | |
B | GLN381 | |
B | GLN479 |
site_id | SWS_FT_FI3 |
Number of Residues | 112 |
Details | BINDING: BINDING => ECO:0000269|PubMed:10319817 |
Chain | Residue | Details |
A | TYR313 | |
A | ILE547 | |
H | ARG325 | |
H | TYR348 | |
H | ARG363 | |
H | ARG375 | |
H | PHE379 | |
H | TYR462 | |
H | GLN484 | |
H | ARG520 | |
H | ILE547 | |
H | ASN575 | |
A | ASN575 | |
H | ARG589 | |
H | VAL595 | |
H | ARG609 | |
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 | |
E | TYR313 | |
E | ARG325 | |
E | TYR348 | |
A | PHE379 | |
E | ARG363 | |
E | ARG375 | |
E | PHE379 | |
E | TYR462 | |
E | GLN484 | |
E | ARG520 | |
E | ILE547 | |
E | ASN575 | |
E | ARG589 | |
E | VAL595 | |
A | TYR462 | |
E | ARG609 | |
F | TYR313 | |
F | ARG325 | |
F | TYR348 | |
F | ARG363 | |
F | ARG375 | |
F | PHE379 | |
F | TYR462 | |
F | GLN484 | |
F | ARG520 | |
A | GLN484 | |
F | ILE547 | |
F | ASN575 | |
F | ARG589 | |
F | VAL595 | |
F | ARG609 | |
G | TYR313 | |
G | ARG325 | |
G | TYR348 | |
G | ARG363 | |
G | ARG375 | |
A | ARG520 | |
G | PHE379 | |
G | TYR462 | |
G | GLN484 | |
G | ARG520 | |
G | ILE547 | |
G | ASN575 | |
G | ARG589 | |
G | VAL595 | |
G | ARG609 | |
H | TYR313 |
site_id | SWS_FT_FI4 |
Number of Residues | 16 |
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 | |
E | HIS385 | |
F | CYS334 | |
F | HIS385 | |
G | CYS334 | |
G | HIS385 | |
H | CYS334 | |
H | HIS385 | |
A | HIS385 | |
B | CYS334 | |
B | HIS385 | |
C | CYS334 | |
C | HIS385 | |
D | CYS334 | |
D | HIS385 | |
E | CYS334 |
site_id | SWS_FT_FI5 |
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 |
Chain | Residue | Details |
A | HIS511 | |
B | HIS511 | |
C | HIS511 | |
D | HIS511 | |
E | HIS511 | |
F | HIS511 | |
G | HIS511 | |
H | HIS511 |
site_id | SWS_FT_FI6 |
Number of Residues | 8 |
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 | |
E | LYS286 | |
F | LYS286 | |
G | LYS286 | |
H | 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 | CSA5 |
Number of Residues | 1 |
Details | Annotated By Reference To The Literature 1qf6 |
Chain | Residue | Details |
E | ARG363 |
site_id | CSA6 |
Number of Residues | 1 |
Details | Annotated By Reference To The Literature 1qf6 |
Chain | Residue | Details |
F | ARG363 |
site_id | CSA7 |
Number of Residues | 1 |
Details | Annotated By Reference To The Literature 1qf6 |
Chain | Residue | Details |
G | ARG363 |
site_id | CSA8 |
Number of Residues | 1 |
Details | Annotated By Reference To The Literature 1qf6 |
Chain | Residue | Details |
H | 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 |
site_id | MCSA5 |
Number of Residues | 7 |
Details | M-CSA 540 |
Chain | Residue | Details |
E | CYS334 | electrostatic stabiliser, metal ligand |
E | ARG363 | electrostatic stabiliser |
E | GLN381 | electrostatic stabiliser |
E | ASP383 | electrostatic stabiliser |
E | HIS385 | metal ligand |
E | LYS465 | electrostatic stabiliser |
E | HIS511 | metal ligand |
site_id | MCSA6 |
Number of Residues | 7 |
Details | M-CSA 540 |
Chain | Residue | Details |
F | CYS334 | electrostatic stabiliser, metal ligand |
F | ARG363 | electrostatic stabiliser |
F | GLN381 | electrostatic stabiliser |
F | ASP383 | electrostatic stabiliser |
F | HIS385 | metal ligand |
F | LYS465 | electrostatic stabiliser |
F | HIS511 | metal ligand |
site_id | MCSA7 |
Number of Residues | 7 |
Details | M-CSA 540 |
Chain | Residue | Details |
G | CYS334 | electrostatic stabiliser, metal ligand |
G | ARG363 | electrostatic stabiliser |
G | GLN381 | electrostatic stabiliser |
G | ASP383 | electrostatic stabiliser |
G | HIS385 | metal ligand |
G | LYS465 | electrostatic stabiliser |
G | HIS511 | metal ligand |
site_id | MCSA8 |
Number of Residues | 7 |
Details | M-CSA 540 |
Chain | Residue | Details |
H | CYS334 | electrostatic stabiliser, metal ligand |
H | ARG363 | electrostatic stabiliser |
H | GLN381 | electrostatic stabiliser |
H | ASP383 | electrostatic stabiliser |
H | HIS385 | metal ligand |
H | LYS465 | electrostatic stabiliser |
H | HIS511 | metal ligand |