4RRF
Editing domain of threonyl-tRNA synthetase from Methanococcus jannaschii with L-Ser3AA
Functional Information from GO Data
Chain | GOid | namespace | contents |
A | 0004829 | molecular_function | threonine-tRNA ligase activity |
A | 0005524 | molecular_function | ATP binding |
A | 0005737 | cellular_component | cytoplasm |
A | 0008270 | molecular_function | zinc ion binding |
B | 0004829 | molecular_function | threonine-tRNA ligase activity |
B | 0005524 | molecular_function | ATP binding |
B | 0005737 | cellular_component | cytoplasm |
B | 0008270 | molecular_function | zinc ion binding |
C | 0004829 | molecular_function | threonine-tRNA ligase activity |
C | 0005524 | molecular_function | ATP binding |
C | 0005737 | cellular_component | cytoplasm |
C | 0008270 | molecular_function | zinc ion binding |
D | 0004829 | molecular_function | threonine-tRNA ligase activity |
D | 0005524 | molecular_function | ATP binding |
D | 0005737 | cellular_component | cytoplasm |
D | 0008270 | molecular_function | zinc ion binding |
E | 0004829 | molecular_function | threonine-tRNA ligase activity |
E | 0005524 | molecular_function | ATP binding |
E | 0005737 | cellular_component | cytoplasm |
E | 0008270 | molecular_function | zinc ion binding |
F | 0004829 | molecular_function | threonine-tRNA ligase activity |
F | 0005524 | molecular_function | ATP binding |
F | 0005737 | cellular_component | cytoplasm |
F | 0008270 | molecular_function | zinc ion binding |
Functional Information from PDB Data
site_id | AC1 |
Number of Residues | 19 |
Details | BINDING SITE FOR RESIDUE A3S A 501 |
Chain | Residue |
A | ILE25 |
A | ALA95 |
A | PHE118 |
A | GLY119 |
A | TRP120 |
A | TYR121 |
A | LYS122 |
A | HOH607 |
A | HOH686 |
D | GLU135 |
D | HOH301 |
A | ILE44 |
A | VAL46 |
A | PRO81 |
A | TYR82 |
A | ALA83 |
A | HIS84 |
A | LEU89 |
A | SER90 |
site_id | AC2 |
Number of Residues | 4 |
Details | BINDING SITE FOR RESIDUE CL A 502 |
Chain | Residue |
A | GLU27 |
A | THR29 |
A | ARG115 |
A | PHE118 |
site_id | AC3 |
Number of Residues | 15 |
Details | BINDING SITE FOR RESIDUE A3S B 201 |
Chain | Residue |
B | ILE44 |
B | VAL46 |
B | PRO81 |
B | TYR82 |
B | ALA83 |
B | LEU89 |
B | SER90 |
B | ALA95 |
B | PHE118 |
B | GLY119 |
B | TYR121 |
B | HOH304 |
B | HOH321 |
B | HOH361 |
C | GLU135 |
site_id | AC4 |
Number of Residues | 13 |
Details | BINDING SITE FOR RESIDUE A3S C 201 |
Chain | Residue |
B | GLU135 |
C | ILE25 |
C | ILE44 |
C | VAL46 |
C | TYR82 |
C | ALA83 |
C | LEU89 |
C | SER90 |
C | ALA95 |
C | PHE118 |
C | GLY119 |
C | HOH303 |
C | HOH342 |
site_id | AC5 |
Number of Residues | 5 |
Details | BINDING SITE FOR RESIDUE MG C 202 |
Chain | Residue |
B | HOH333 |
B | HOH363 |
C | HOH322 |
C | HOH329 |
C | HOH355 |
site_id | AC6 |
Number of Residues | 15 |
Details | BINDING SITE FOR RESIDUE A3S D 201 |
Chain | Residue |
A | GLU135 |
D | ILE25 |
D | ILE44 |
D | VAL46 |
D | TYR82 |
D | ALA83 |
D | HIS84 |
D | LEU89 |
D | SER90 |
D | ALA95 |
D | PHE118 |
D | GLY119 |
D | HOH302 |
D | HOH315 |
D | HOH374 |
site_id | AC7 |
Number of Residues | 6 |
Details | BINDING SITE FOR RESIDUE MG D 202 |
Chain | Residue |
A | HOH627 |
D | HOH305 |
D | HOH316 |
D | HOH333 |
D | HOH350 |
D | HOH366 |
site_id | AC8 |
Number of Residues | 17 |
Details | BINDING SITE FOR RESIDUE A3S E 201 |
Chain | Residue |
E | ILE25 |
E | ILE44 |
E | VAL46 |
E | PRO81 |
E | TYR82 |
E | ALA83 |
E | HIS84 |
E | LEU89 |
E | SER90 |
E | ALA95 |
E | PHE118 |
E | GLY119 |
E | TYR121 |
E | HOH309 |
E | HOH333 |
E | HOH354 |
F | GLU135 |
site_id | AC9 |
Number of Residues | 15 |
Details | BINDING SITE FOR RESIDUE A3S F 201 |
Chain | Residue |
F | TYR82 |
F | ALA83 |
F | HIS84 |
F | SER90 |
F | ALA95 |
F | PHE118 |
F | GLY119 |
F | TYR121 |
F | LYS122 |
F | HOH306 |
E | GLU135 |
F | ILE25 |
F | ILE44 |
F | ALA45 |
F | VAL46 |