4KR3
Glycyl-tRNA synthetase mutant E71G in complex with tRNA-Gly
Functional Information from GO Data
Chain | GOid | namespace | contents |
A | 0000166 | molecular_function | nucleotide binding |
A | 0004812 | molecular_function | aminoacyl-tRNA ligase activity |
A | 0004820 | molecular_function | glycine-tRNA ligase activity |
A | 0005524 | molecular_function | ATP binding |
A | 0005737 | cellular_component | cytoplasm |
A | 0006418 | biological_process | tRNA aminoacylation for protein translation |
A | 0006426 | biological_process | glycyl-tRNA aminoacylation |
Functional Information from PDB Data
site_id | AC1 |
Number of Residues | 6 |
Details | BINDING SITE FOR RESIDUE GLY A 701 |
Chain | Residue |
A | GLU245 |
A | GLU296 |
A | ARG410 |
A | GLU522 |
A | SER524 |
A | ANP702 |
site_id | AC2 |
Number of Residues | 15 |
Details | BINDING SITE FOR RESIDUE ANP A 702 |
Chain | Residue |
A | ILE287 |
A | ARG288 |
A | VAL289 |
A | PHE292 |
A | HIS378 |
A | ASP392 |
A | GLU403 |
A | ILE404 |
A | SER524 |
A | GLY526 |
A | ARG529 |
A | GLY701 |
A | ARG277 |
A | GLU279 |
A | LEU286 |
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 |