4JYZ
Crystal structure of E. coli glutaminyl-tRNA synthetase bound to ATP and native tRNA(Gln) containing the cmnm5s2U34 anticodon wobble base
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0000166 | molecular_function | nucleotide binding |
| A | 0004812 | molecular_function | aminoacyl-tRNA ligase activity |
| A | 0004819 | molecular_function | glutamine-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 | 0006424 | biological_process | glutamyl-tRNA aminoacylation |
| A | 0006425 | biological_process | glutaminyl-tRNA aminoacylation |
| A | 0016874 | molecular_function | ligase activity |
| A | 0043039 | biological_process | tRNA aminoacylation |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 13 |
| Details | BINDING SITE FOR RESIDUE ATP A 601 |
| Chain | Residue |
| A | PRO32 |
| A | MET268 |
| A | LYS270 |
| A | HOH705 |
| B | A976 |
| A | GLU34 |
| A | HIS40 |
| A | GLY42 |
| A | HIS43 |
| A | SER46 |
| A | THR230 |
| A | ARG260 |
| A | LEU261 |
| site_id | AC2 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE SO4 A 602 |
| Chain | Residue |
| A | VAL267 |
| A | MET268 |
| A | SER269 |
| A | LYS272 |
| A | GLY482 |
| A | HOH771 |
| site_id | AC3 |
| Number of Residues | 3 |
| Details | BINDING SITE FOR RESIDUE SO4 A 603 |
| Chain | Residue |
| A | MET290 |
| A | LEU296 |
| A | MET324 |
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 |
| A | PRO33-ALA44 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 7 |
| Details | Region: {"description":"Interaction with tRNA","evidences":[{"source":"HAMAP-Rule","id":"MF_00126","evidenceCode":"ECO:0000255"},{"source":"PubMed","id":"23727144","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"9562563","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI2 |
| Number of Residues | 10 |
| Details | Motif: {"description":"'HIGH' region","evidences":[{"source":"HAMAP-Rule","id":"MF_00126","evidenceCode":"ECO:0000255"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI3 |
| Number of Residues | 4 |
| Details | Motif: {"description":"'KMSKS' region","evidences":[{"source":"HAMAP-Rule","id":"MF_00126","evidenceCode":"ECO:0000255"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI4 |
| Number of Residues | 8 |
| Details | Binding site: {"evidences":[{"source":"HAMAP-Rule","id":"MF_00126","evidenceCode":"ECO:0000255"},{"source":"PubMed","id":"23727144","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"4JXX","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"4JXZ","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"4JYZ","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI5 |
| Number of Residues | 1 |
| Details | Binding site: {"evidences":[{"source":"HAMAP-Rule","id":"MF_00126","evidenceCode":"ECO:0000255"},{"source":"PubMed","id":"12691748","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"18477696","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"9562563","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"1O0B","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI6 |
| Number of Residues | 1 |
| Details | Binding site: {"evidences":[{"source":"HAMAP-Rule","id":"MF_00126","evidenceCode":"ECO:0000255"},{"source":"PubMed","id":"12691748","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"15845536","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"18477696","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"9562563","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"1O0B","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"1ZJW","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI7 |
| Number of Residues | 4 |
| Details | Binding site: {"evidences":[{"source":"HAMAP-Rule","id":"MF_00126","evidenceCode":"ECO:0000255"},{"source":"PubMed","id":"18477696","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"23727144","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"9562563","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"4JXX","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"4JXZ","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"4JYZ","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
Catalytic Information from CSA
| site_id | MCSA1 |
| Number of Residues | 3 |
| Details | M-CSA 850 |
| Chain | Residue | Details |
| A | GLU34 | proton shuttle (general acid/base) |
| A | ARG260 | electrostatic stabiliser |
| A | LYS270 | electrostatic stabiliser |






