3AL0
Crystal structure of the glutamine transamidosome from Thermotoga maritima in the glutamylation state.
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0000166 | molecular_function | nucleotide binding |
| A | 0003824 | molecular_function | catalytic activity |
| A | 0005524 | molecular_function | ATP binding |
| A | 0006412 | biological_process | translation |
| A | 0016874 | molecular_function | ligase activity |
| A | 0030956 | cellular_component | glutamyl-tRNA(Gln) amidotransferase complex |
| A | 0050567 | molecular_function | glutaminyl-tRNA synthase (glutamine-hydrolyzing) activity |
| B | 0000166 | molecular_function | nucleotide binding |
| B | 0003824 | molecular_function | catalytic activity |
| B | 0005524 | molecular_function | ATP binding |
| B | 0006412 | biological_process | translation |
| B | 0016874 | molecular_function | ligase activity |
| B | 0016884 | molecular_function | carbon-nitrogen ligase activity, with glutamine as amido-N-donor |
| B | 0050566 | molecular_function | asparaginyl-tRNA synthase (glutamine-hydrolyzing) activity |
| B | 0050567 | molecular_function | glutaminyl-tRNA synthase (glutamine-hydrolyzing) activity |
| B | 0070681 | biological_process | glutaminyl-tRNAGln biosynthesis via transamidation |
| C | 0000049 | molecular_function | tRNA binding |
| C | 0000166 | molecular_function | nucleotide binding |
| C | 0004812 | molecular_function | aminoacyl-tRNA ligase activity |
| C | 0004818 | molecular_function | glutamate-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 | 0006424 | biological_process | glutamyl-tRNA aminoacylation |
| C | 0006450 | biological_process | regulation of translational fidelity |
| C | 0008270 | molecular_function | zinc ion binding |
| C | 0016874 | molecular_function | ligase activity |
| C | 0043039 | biological_process | tRNA aminoacylation |
| C | 0050566 | molecular_function | asparaginyl-tRNA synthase (glutamine-hydrolyzing) activity |
| C | 0050567 | molecular_function | glutaminyl-tRNA synthase (glutamine-hydrolyzing) activity |
| C | 0070681 | biological_process | glutaminyl-tRNAGln biosynthesis via transamidation |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 17 |
| Details | BINDING SITE FOR RESIDUE GSU C 1001 |
| Chain | Residue |
| C | ARG132 |
| C | GLY321 |
| C | ASP323 |
| C | HIS324 |
| C | LEU350 |
| C | ILE351 |
| C | LEU359 |
| C | LYS361 |
| E | A76 |
| C | ALA134 |
| C | PRO135 |
| C | SER136 |
| C | GLY144 |
| C | THR148 |
| C | GLU168 |
| C | TYR302 |
| C | ARG320 |
| site_id | AC2 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE ZN B 1001 |
| Chain | Residue |
| B | CYS23 |
| B | CYS25 |
| B | CYS39 |
| B | CYS42 |
Functional Information from PROSITE/UniProt
| site_id | PS00178 |
| Number of Residues | 12 |
| Details | AA_TRNA_LIGASE_I Aminoacyl-transfer RNA synthetases class-I signature. PspTGhLHVGGA |
| Chain | Residue | Details |
| C | PRO135-ALA146 |
| site_id | PS00571 |
| Number of Residues | 32 |
| Details | AMIDASES Amidases signature. GGSSGGsAAaVSagmvvaAlGsDtGgSVRqPA |
| Chain | Residue | Details |
| A | GLY139-ALA170 |
| site_id | PS01234 |
| Number of Residues | 15 |
| Details | GATB Glutamyl-tRNA(Gln) amidotransferase subunit B signature. MNRcgvPLIEIvTeP |
| Chain | Residue | Details |
| B | MET148-PRO162 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 2 |
| Details | Active site: {"description":"Charge relay system","evidences":[{"evidenceCode":"ECO:0000250"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI2 |
| Number of Residues | 1 |
| Details | Active site: {"description":"Acyl-ester intermediate","evidences":[{"evidenceCode":"ECO:0000250"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI3 |
| Number of Residues | 10 |
| Details | Motif: {"description":"'HIGH' region","evidences":[{"source":"HAMAP-Rule","id":"MF_00022","evidenceCode":"ECO:0000255"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI4 |
| Number of Residues | 4 |
| Details | Motif: {"description":"'KMSKS' region","evidences":[{"source":"HAMAP-Rule","id":"MF_00022","evidenceCode":"ECO:0000255"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI5 |
| Number of Residues | 1 |
| Details | Binding site: {"evidences":[{"source":"HAMAP-Rule","id":"MF_00022","evidenceCode":"ECO:0000255"}]} |
| Chain | Residue | Details |
