1MB2
Crystal Structure of Tryptophanyl-tRNA Synthetase Complexed with Tryptophan in an Open Conformation
Functional Information from GO Data
Chain | GOid | namespace | contents |
A | 0000166 | molecular_function | nucleotide binding |
A | 0004812 | molecular_function | aminoacyl-tRNA ligase activity |
A | 0004830 | molecular_function | tryptophan-tRNA ligase activity |
A | 0005524 | molecular_function | ATP binding |
A | 0005737 | cellular_component | cytoplasm |
A | 0005829 | cellular_component | cytosol |
A | 0006412 | biological_process | translation |
A | 0006418 | biological_process | tRNA aminoacylation for protein translation |
A | 0006436 | biological_process | tryptophanyl-tRNA aminoacylation |
B | 0000166 | molecular_function | nucleotide binding |
B | 0004812 | molecular_function | aminoacyl-tRNA ligase activity |
B | 0004830 | molecular_function | tryptophan-tRNA ligase activity |
B | 0005524 | molecular_function | ATP binding |
B | 0005737 | cellular_component | cytoplasm |
B | 0005829 | cellular_component | cytosol |
B | 0006412 | biological_process | translation |
B | 0006418 | biological_process | tRNA aminoacylation for protein translation |
B | 0006436 | biological_process | tryptophanyl-tRNA aminoacylation |
C | 0000166 | molecular_function | nucleotide binding |
C | 0004812 | molecular_function | aminoacyl-tRNA ligase activity |
C | 0004830 | molecular_function | tryptophan-tRNA ligase activity |
C | 0005524 | molecular_function | ATP binding |
C | 0005737 | cellular_component | cytoplasm |
C | 0005829 | cellular_component | cytosol |
C | 0006412 | biological_process | translation |
C | 0006418 | biological_process | tRNA aminoacylation for protein translation |
C | 0006436 | biological_process | tryptophanyl-tRNA aminoacylation |
D | 0000166 | molecular_function | nucleotide binding |
D | 0004812 | molecular_function | aminoacyl-tRNA ligase activity |
D | 0004830 | molecular_function | tryptophan-tRNA ligase activity |
D | 0005524 | molecular_function | ATP binding |
D | 0005737 | cellular_component | cytoplasm |
D | 0005829 | cellular_component | cytosol |
D | 0006412 | biological_process | translation |
D | 0006418 | biological_process | tRNA aminoacylation for protein translation |
D | 0006436 | biological_process | tryptophanyl-tRNA aminoacylation |
E | 0000166 | molecular_function | nucleotide binding |
E | 0004812 | molecular_function | aminoacyl-tRNA ligase activity |
E | 0004830 | molecular_function | tryptophan-tRNA ligase activity |
E | 0005524 | molecular_function | ATP binding |
E | 0005737 | cellular_component | cytoplasm |
E | 0005829 | cellular_component | cytosol |
E | 0006412 | biological_process | translation |
E | 0006418 | biological_process | tRNA aminoacylation for protein translation |
E | 0006436 | biological_process | tryptophanyl-tRNA aminoacylation |
F | 0000166 | molecular_function | nucleotide binding |
F | 0004812 | molecular_function | aminoacyl-tRNA ligase activity |
F | 0004830 | molecular_function | tryptophan-tRNA ligase activity |
F | 0005524 | molecular_function | ATP binding |
F | 0005737 | cellular_component | cytoplasm |
F | 0005829 | cellular_component | cytosol |
F | 0006412 | biological_process | translation |
F | 0006418 | biological_process | tRNA aminoacylation for protein translation |
F | 0006436 | biological_process | tryptophanyl-tRNA aminoacylation |
Functional Information from PDB Data
site_id | AC1 |
Number of Residues | 8 |
Details | BINDING SITE FOR RESIDUE TRP A 400 |
Chain | Residue |
A | PHE5 |
A | GLY7 |
A | VAL40 |
A | HIS43 |
A | MET129 |
A | ASP132 |
A | VAL143 |
A | GLN147 |
site_id | AC2 |
Number of Residues | 8 |
Details | BINDING SITE FOR RESIDUE TRP B 401 |
Chain | Residue |
B | GLY7 |
B | GLN9 |
B | VAL40 |
B | HIS43 |
B | MET129 |
B | ASP132 |
B | GLN147 |
B | PHE5 |
site_id | AC3 |
Number of Residues | 8 |
Details | BINDING SITE FOR RESIDUE TRP C 402 |
Chain | Residue |
C | PHE5 |
C | GLY7 |
C | VAL40 |
C | HIS43 |
C | MET129 |
C | ASP132 |
C | VAL143 |
C | GLN147 |
site_id | AC4 |
Number of Residues | 9 |
Details | BINDING SITE FOR RESIDUE TRP D 403 |
Chain | Residue |
D | PHE5 |
D | GLY7 |
D | GLN9 |
D | VAL40 |
D | HIS43 |
D | MET129 |
D | ASP132 |
D | VAL141 |
D | GLN147 |
site_id | AC5 |
Number of Residues | 7 |
Details | BINDING SITE FOR RESIDUE TRP E 404 |
Chain | Residue |
E | PHE5 |
E | GLY7 |
E | HIS43 |
E | MET129 |
E | ASP132 |
E | VAL143 |
E | GLN147 |
site_id | AC6 |
Number of Residues | 8 |
Details | BINDING SITE FOR RESIDUE TRP F 405 |
Chain | Residue |
F | PHE5 |
F | GLY7 |
F | GLN9 |
F | HIS43 |
F | MET129 |
F | ASP132 |
F | VAL143 |
F | GLN147 |
Functional Information from PROSITE/UniProt
site_id | PS00178 |
Number of Residues | 10 |
Details | AA_TRNA_LIGASE_I Aminoacyl-transfer RNA synthetases class-I signature. P..SGvITIGNY |
Chain | Residue | Details |
A | PRO10-TYR19 |
Functional Information from SwissProt/UniProt
site_id | SWS_FT_FI1 |
Number of Residues | 36 |
Details | BINDING: BINDING => ECO:0000255|HAMAP-Rule:MF_00140, ECO:0000269|PubMed:26555258, ECO:0007744|PDB:5DK4 |
Chain | Residue | Details |
A | GLN9 | |
B | GLY144 | |
B | ILE183 | |
B | LYS192 | |
C | GLN9 | |
C | GLY17 | |
C | ASP132 | |
C | GLY144 | |
C | ILE183 | |
C | LYS192 | |
D | GLN9 | |
A | GLY17 | |
D | GLY17 | |
D | ASP132 | |
D | GLY144 | |
D | ILE183 | |
D | LYS192 | |
E | GLN9 | |
E | GLY17 | |
E | ASP132 | |
E | GLY144 | |
E | ILE183 | |
A | ASP132 | |
E | LYS192 | |
F | GLN9 | |
F | GLY17 | |
F | ASP132 | |
F | GLY144 | |
F | ILE183 | |
F | LYS192 | |
A | GLY144 | |
A | ILE183 | |
A | LYS192 | |
B | GLN9 | |
B | GLY17 | |
B | ASP132 |
Catalytic Information from CSA
site_id | MCSA1 |
Number of Residues | 3 |
Details | M-CSA 481 |
Chain | Residue | Details |
A | LYS111 | electrostatic stabiliser |
A | LYS192 | electrostatic stabiliser |
A | LYS195 | electrostatic stabiliser |
site_id | MCSA2 |
Number of Residues | 3 |
Details | M-CSA 481 |
Chain | Residue | Details |
B | LYS111 | electrostatic stabiliser |
B | LYS192 | electrostatic stabiliser |
B | LYS195 | electrostatic stabiliser |
site_id | MCSA3 |
Number of Residues | 3 |
Details | M-CSA 481 |
Chain | Residue | Details |
C | LYS111 | electrostatic stabiliser |
C | LYS192 | electrostatic stabiliser |
C | LYS195 | electrostatic stabiliser |
site_id | MCSA4 |
Number of Residues | 3 |
Details | M-CSA 481 |
Chain | Residue | Details |
D | LYS111 | electrostatic stabiliser |
D | LYS192 | electrostatic stabiliser |
D | LYS195 | electrostatic stabiliser |
site_id | MCSA5 |
Number of Residues | 3 |
Details | M-CSA 481 |
Chain | Residue | Details |
E | LYS111 | electrostatic stabiliser |
E | LYS192 | electrostatic stabiliser |
E | LYS195 | electrostatic stabiliser |
site_id | MCSA6 |
Number of Residues | 3 |
Details | M-CSA 481 |
Chain | Residue | Details |
F | LYS111 | electrostatic stabiliser |
F | LYS192 | electrostatic stabiliser |
F | LYS195 | electrostatic stabiliser |