1D2R
2.9 A CRYSTAL STRUCTURE OF LIGAND-FREE TRYPTOPHANYL-TRNA SYNTHETASE: DOMAIN MOVEMENTS FRAGMENT THE ADENINE NUCLEOTIDE BINDING SITE.
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 |
| A | 0016874 | molecular_function | ligase activity |
| 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 |
| B | 0016874 | molecular_function | ligase activity |
| 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 |
| C | 0016874 | molecular_function | ligase activity |
| 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 |
| D | 0016874 | molecular_function | ligase activity |
| 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 |
| E | 0016874 | molecular_function | ligase activity |
| 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 |
| F | 0016874 | molecular_function | ligase activity |
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 | 48 |
| Details | Motif: {"description":"'HIGH' region","evidences":[{"source":"HAMAP-Rule","id":"MF_00140","evidenceCode":"ECO:0000255"},{"evidenceCode":"ECO:0000305"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI2 |
| Number of Residues | 24 |
| Details | Motif: {"description":"'KMSKS' region","evidences":[{"source":"HAMAP-Rule","id":"MF_00140","evidenceCode":"ECO:0000255"},{"evidenceCode":"ECO:0000305"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI3 |
| Number of Residues | 66 |
| Details | Binding site: {"evidences":[{"source":"HAMAP-Rule","id":"MF_00140","evidenceCode":"ECO:0000255"},{"source":"PubMed","id":"26555258","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"5DK4","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
Catalytic Information from CSA
| site_id | CSA1 |
| Number of Residues | 2 |
| Details | a catalytic site defined by CSA, PubMed 12473451 |
| Chain | Residue | Details |
| A | LYS192 | |
| A | LYS195 |
| site_id | CSA2 |
| Number of Residues | 2 |
| Details | a catalytic site defined by CSA, PubMed 12473451 |
| Chain | Residue | Details |
| B | LYS192 | |
| B | LYS195 |
| site_id | CSA3 |
| Number of Residues | 2 |
| Details | a catalytic site defined by CSA, PubMed 12473451 |
| Chain | Residue | Details |
| C | LYS192 | |
| C | LYS195 |
| site_id | CSA4 |
| Number of Residues | 2 |
| Details | a catalytic site defined by CSA, PubMed 12473451 |
| Chain | Residue | Details |
| D | LYS192 | |
| D | LYS195 |
| site_id | CSA5 |
| Number of Residues | 2 |
| Details | a catalytic site defined by CSA, PubMed 12473451 |
| Chain | Residue | Details |
| E | LYS192 | |
| E | LYS195 |
| site_id | CSA6 |
| Number of Residues | 2 |
| Details | a catalytic site defined by CSA, PubMed 12473451 |
| Chain | Residue | Details |
| F | LYS192 | |
| F | LYS195 |
| 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 |
