2PME
The Apo crystal Structure of the glycyl-tRNA synthetase
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 |
A | 0141192 | molecular_function | ATP:ATP adenylyltransferase activity |
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 | ARG277 | |
A | GLU403 |
site_id | SWS_FT_FI3 |
Number of Residues | 2 |
Details | BINDING: BINDING => ECO:0000269|PubMed:19710017, ECO:0007744|PDB:2ZT7 |
Chain | Residue | Details |
A | ARG288 | |
A | ARG529 |
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 | LYS150 | |
A | LYS447 |
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 |
Catalytic Information from CSA
site_id | CSA1 |
Number of Residues | 1 |
Details | Annotated By Reference To The Literature 1qf6 |
Chain | Residue | Details |
A | ARG277 |