2D6F
Crystal structure of Glu-tRNA(Gln) amidotransferase in the complex with tRNA(Gln)
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0000166 | molecular_function | nucleotide binding |
| A | 0004067 | molecular_function | asparaginase activity |
| A | 0005524 | molecular_function | ATP binding |
| A | 0006412 | biological_process | translation |
| A | 0006450 | biological_process | regulation of translational fidelity |
| A | 0006520 | biological_process | amino acid metabolic process |
| A | 0016874 | molecular_function | ligase activity |
| A | 0050567 | molecular_function | glutaminyl-tRNA synthase (glutamine-hydrolyzing) activity |
| B | 0000166 | molecular_function | nucleotide binding |
| B | 0004067 | molecular_function | asparaginase activity |
| B | 0005524 | molecular_function | ATP binding |
| B | 0006412 | biological_process | translation |
| B | 0006450 | biological_process | regulation of translational fidelity |
| B | 0006520 | biological_process | amino acid metabolic process |
| B | 0016874 | molecular_function | ligase activity |
| B | 0050567 | molecular_function | glutaminyl-tRNA synthase (glutamine-hydrolyzing) activity |
| C | 0000166 | molecular_function | nucleotide binding |
| C | 0003824 | molecular_function | catalytic activity |
| C | 0004812 | molecular_function | aminoacyl-tRNA ligase activity |
| C | 0005524 | molecular_function | ATP binding |
| C | 0005737 | cellular_component | cytoplasm |
| C | 0006412 | biological_process | translation |
| C | 0016874 | molecular_function | ligase activity |
| C | 0016884 | molecular_function | carbon-nitrogen ligase activity, with glutamine as amido-N-donor |
| C | 0050567 | molecular_function | glutaminyl-tRNA synthase (glutamine-hydrolyzing) activity |
| C | 0070681 | biological_process | glutaminyl-tRNAGln biosynthesis via transamidation |
| D | 0000166 | molecular_function | nucleotide binding |
| D | 0003824 | molecular_function | catalytic activity |
| D | 0004812 | molecular_function | aminoacyl-tRNA ligase activity |
| D | 0005524 | molecular_function | ATP binding |
| D | 0005737 | cellular_component | cytoplasm |
| D | 0006412 | biological_process | translation |
| D | 0016874 | molecular_function | ligase activity |
| D | 0016884 | molecular_function | carbon-nitrogen ligase activity, with glutamine as amido-N-donor |
| D | 0050567 | molecular_function | glutaminyl-tRNA synthase (glutamine-hydrolyzing) activity |
| D | 0070681 | biological_process | glutaminyl-tRNAGln biosynthesis via transamidation |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE ZN C 900 |
| Chain | Residue |
| C | CYS26 |
| C | CYS28 |
| C | CYS79 |
| C | GLU82 |
| site_id | AC2 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE ZN D 1900 |
| Chain | Residue |
| D | CYS26 |
| D | CYS28 |
| D | CYS79 |
| D | GLU82 |
Functional Information from PROSITE/UniProt
| site_id | PS00144 |
| Number of Residues | 9 |
| Details | ASN_GLN_ASE_1 Asparaginase / glutaminase active site signature 1. IiSTGGTVA |
| Chain | Residue | Details |
| A | ILE95-ALA103 |
| site_id | PS00917 |
| Number of Residues | 11 |
| Details | ASN_GLN_ASE_2 Asparaginase / glutaminase active site signature 2. GvVvaHGTDTM |
| Chain | Residue | Details |
| A | GLY170-MET180 |
| site_id | PS01234 |
| Number of Residues | 15 |
| Details | GATB Glutamyl-tRNA(Gln) amidotransferase subunit B signature. LDRlgiPLVEItTdP |
| Chain | Residue | Details |
| C | LEU175-PRO189 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 656 |
| Details | Domain: {"description":"Asparaginase/glutaminase","evidences":[{"source":"PROSITE-ProRule","id":"PRU01068","evidenceCode":"ECO:0000255"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI2 |
| Number of Residues | 8 |
| Details | Active site: {"evidences":[{"evidenceCode":"ECO:0000250"}]} |
| Chain | Residue | Details |
Catalytic Information from CSA
| site_id | CSA1 |
| Number of Residues | 1 |
| Details | Annotated By Reference To The Literature 1djo |
| Chain | Residue | Details |
| A | SER374 |
| site_id | CSA2 |
| Number of Residues | 1 |
| Details | Annotated By Reference To The Literature 1djo |
| Chain | Residue | Details |
| B | SER374 |
| site_id | CSA3 |
| Number of Residues | 1 |
| Details | Annotated By Reference To The Literature 1djo |
| Chain | Residue | Details |
| A | GLY376 |
| site_id | CSA4 |
| Number of Residues | 1 |
| Details | Annotated By Reference To The Literature 1djo |
| Chain | Residue | Details |
| B | GLY376 |
