4KQE
The mutant structure of the human glycyl-tRNA synthetase E71G
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0000166 | molecular_function | nucleotide binding |
| A | 0004081 | molecular_function | bis(5'-nucleosyl)-tetraphosphatase (asymmetrical) activity |
| A | 0004812 | molecular_function | aminoacyl-tRNA ligase activity |
| A | 0004820 | molecular_function | glycine-tRNA ligase activity |
| A | 0005515 | molecular_function | protein binding |
| A | 0005524 | molecular_function | ATP binding |
| A | 0005576 | cellular_component | extracellular region |
| A | 0005737 | cellular_component | cytoplasm |
| A | 0005739 | cellular_component | mitochondrion |
| A | 0005759 | cellular_component | mitochondrial matrix |
| A | 0005829 | cellular_component | cytosol |
| A | 0006412 | biological_process | translation |
| A | 0006418 | biological_process | tRNA aminoacylation for protein translation |
| A | 0006426 | biological_process | glycyl-tRNA aminoacylation |
| A | 0015966 | biological_process | diadenosine tetraphosphate biosynthetic process |
| A | 0016740 | molecular_function | transferase activity |
| A | 0016787 | molecular_function | hydrolase activity |
| A | 0030141 | cellular_component | secretory granule |
| A | 0030424 | cellular_component | axon |
| A | 0042802 | molecular_function | identical protein binding |
| A | 0042995 | cellular_component | cell projection |
| A | 0046983 | molecular_function | protein dimerization activity |
| A | 0070062 | cellular_component | extracellular exosome |
| A | 0070150 | biological_process | mitochondrial glycyl-tRNA aminoacylation |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 3 |
| Details | BINDING SITE FOR RESIDUE GOL A 701 |
| Chain | Residue |
| A | ASP621 |
| A | PRO627 |
| A | THR629 |
Functional Information from PROSITE/UniProt
| site_id | PS00762 |
| Number of Residues | 29 |
| Details | WHEP_TRS_1 WHEP-TRS domain signature. QGDlVRklKedKApqvdVDkaVaeLkarK |
| Chain | Residue | Details |
| A | GLN20-LYS48 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 2 |
| Details | BINDING: BINDING => ECO:0000269|PubMed:19710017, ECO:0000269|PubMed:24898252, ECO:0000305|PubMed:27261259, ECO:0007744|PDB:2ZT7, ECO:0007744|PDB:4KR3 |
| Chain | Residue | Details |
| A | GLU245 | |
| A | GLU296 |
| site_id | SWS_FT_FI2 |
| Number of Residues | 2 |
| Details | BINDING: BINDING => ECO:0000269|PubMed:19710017, ECO:0000305|PubMed:24898252, ECO:0000305|PubMed:27261259, ECO:0007744|PDB:2ZT7 |
| Chain | Residue | Details |
| A | GLU403 | |
| A | ARG277 |
| site_id | SWS_FT_FI3 |
| Number of Residues | 2 |
| Details | BINDING: BINDING => ECO:0000269|PubMed:19710017, ECO:0007744|PDB:2ZT7 |
| Chain | Residue | Details |
| A | ARG529 | |
| A | ARG288 |
| site_id | SWS_FT_FI4 |
| Number of Residues | 1 |
| Details | BINDING: BINDING => ECO:0000269|PubMed:19710017, ECO:0000269|PubMed:24898252, ECO:0007744|PDB:2ZT7, ECO:0007744|PDB:4KR3 |
| Chain | Residue | Details |
| A | GLU522 |
| site_id | SWS_FT_FI5 |
| Number of Residues | 2 |
| Details | MOD_RES: N6-acetyllysine => ECO:0007744|PubMed:19608861 |
| Chain | Residue | Details |
| A | LYS447 | |
| A | LYS150 |
| site_id | SWS_FT_FI6 |
| Number of Residues | 1 |
| Details | MOD_RES: Phosphotyrosine => ECO:0000250|UniProtKB:Q9CZD3 |
| Chain | Residue | Details |
| A | TYR399 |
| site_id | SWS_FT_FI7 |
| Number of Residues | 1 |
| Details | MOD_RES: Phosphoserine => ECO:0000250|UniProtKB:Q9CZD3 |
| Chain | Residue | Details |
| A | SER646 |
| site_id | SWS_FT_FI8 |
| Number of Residues | 1 |
| Details | MOD_RES: Phosphothreonine => ECO:0007744|PubMed:23186163 |
| Chain | Residue | Details |
| A | THR682 |
