1GSG
Structure of E.coli glutaminyl-tRNA synthetase complexed with trnagln and ATP at 2.8 Angstroms resolution
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| P | 0000166 | molecular_function | nucleotide binding |
| P | 0004812 | molecular_function | aminoacyl-tRNA ligase activity |
| P | 0004819 | molecular_function | glutamine-tRNA ligase activity |
| P | 0005524 | molecular_function | ATP binding |
| P | 0005737 | cellular_component | cytoplasm |
| P | 0005829 | cellular_component | cytosol |
| P | 0006412 | biological_process | translation |
| P | 0006418 | biological_process | tRNA aminoacylation for protein translation |
| P | 0006424 | biological_process | glutamyl-tRNA aminoacylation |
| P | 0006425 | biological_process | glutaminyl-tRNA aminoacylation |
| P | 0016874 | molecular_function | ligase activity |
| P | 0043039 | biological_process | tRNA aminoacylation |
Functional Information from PROSITE/UniProt
| site_id | PS00178 |
| Number of Residues | 12 |
| Details | AA_TRNA_LIGASE_I Aminoacyl-transfer RNA synthetases class-I signature. PepNGyLHIGHA |
| Chain | Residue | Details |
| P | PRO33-ALA44 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 2 |
| Details | BINDING: BINDING => ECO:0000255|HAMAP-Rule:MF_00126, ECO:0000269|PubMed:23727144, ECO:0007744|PDB:4JXX, ECO:0007744|PDB:4JXZ, ECO:0007744|PDB:4JYZ |
| Chain | Residue | Details |
| P | PRO35 | |
| P | ILE41 |
| site_id | SWS_FT_FI2 |
| Number of Residues | 1 |
| Details | BINDING: BINDING => ECO:0000255|HAMAP-Rule:MF_00126, ECO:0000269|PubMed:12691748, ECO:0000269|PubMed:18477696, ECO:0000269|PubMed:9562563, ECO:0007744|PDB:1O0B |
| Chain | Residue | Details |
| P | ASP67 |
| site_id | SWS_FT_FI3 |
| Number of Residues | 1 |
| Details | BINDING: BINDING => ECO:0000255|HAMAP-Rule:MF_00126, ECO:0000269|PubMed:12691748, ECO:0000269|PubMed:15845536, ECO:0000269|PubMed:18477696, ECO:0000269|PubMed:9562563, ECO:0007744|PDB:1O0B, ECO:0007744|PDB:1ZJW |
| Chain | Residue | Details |
| P | ASP212 |
| site_id | SWS_FT_FI4 |
| Number of Residues | 3 |
| Details | BINDING: BINDING => ECO:0000255|HAMAP-Rule:MF_00126, ECO:0000269|PubMed:18477696, ECO:0000269|PubMed:23727144, ECO:0000269|PubMed:9562563, ECO:0007744|PDB:4JXX, ECO:0007744|PDB:4JXZ, ECO:0007744|PDB:4JYZ |
| Chain | Residue | Details |
| P | LEU231 | |
| P | LEU261 | |
| P | SER269 |
Catalytic Information from CSA
| site_id | CSA1 |
| Number of Residues | 3 |
| Details | Annotated By Reference To The Literature 1euy |
| Chain | Residue | Details |
| P | GLU34 | |
| P | LYS270 | |
| P | ARG260 |
| site_id | CSA2 |
| Number of Residues | 1 |
| Details | Annotated By Reference To The Literature 1euy |
| Chain | Residue | Details |
| P | LYS270 |
| site_id | MCSA1 |
| Number of Residues | 3 |
| Details | M-CSA 850 |
| Chain | Residue | Details |
| P | PRO35 | proton shuttle (general acid/base) |
| P | LEU261 | electrostatic stabiliser |
| P | ARG271 | electrostatic stabiliser |
