1WLE
Crystal Structure of mammalian mitochondrial seryl-tRNA synthetase complexed with seryl-adenylate
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0000049 | molecular_function | tRNA binding |
| A | 0000166 | molecular_function | nucleotide binding |
| A | 0004812 | molecular_function | aminoacyl-tRNA ligase activity |
| A | 0004828 | molecular_function | serine-tRNA ligase activity |
| A | 0005524 | molecular_function | ATP binding |
| 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 | 0006434 | biological_process | seryl-tRNA aminoacylation |
| A | 0016874 | molecular_function | ligase activity |
| A | 0070158 | biological_process | mitochondrial seryl-tRNA aminoacylation |
| B | 0000049 | molecular_function | tRNA binding |
| B | 0000166 | molecular_function | nucleotide binding |
| B | 0004812 | molecular_function | aminoacyl-tRNA ligase activity |
| B | 0004828 | molecular_function | serine-tRNA ligase activity |
| B | 0005524 | molecular_function | ATP binding |
| B | 0005739 | cellular_component | mitochondrion |
| B | 0005759 | cellular_component | mitochondrial matrix |
| B | 0005829 | cellular_component | cytosol |
| B | 0006412 | biological_process | translation |
| B | 0006418 | biological_process | tRNA aminoacylation for protein translation |
| B | 0006434 | biological_process | seryl-tRNA aminoacylation |
| B | 0016874 | molecular_function | ligase activity |
| B | 0070158 | biological_process | mitochondrial seryl-tRNA aminoacylation |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 20 |
| Details | BINDING SITE FOR RESIDUE SRP A 900 |
| Chain | Residue |
| A | THR282 |
| A | GLU401 |
| A | VAL402 |
| A | THR403 |
| A | SER404 |
| A | ASN434 |
| A | THR436 |
| A | ALA439 |
| A | HOH902 |
| A | HOH954 |
| A | HOH1040 |
| A | GLU284 |
| A | HOH1134 |
| A | ARG313 |
| A | GLU315 |
| A | TYR326 |
| A | ARG327 |
| A | VAL328 |
| A | PHE331 |
| A | GLU335 |
| site_id | AC2 |
| Number of Residues | 18 |
| Details | BINDING SITE FOR RESIDUE SRP B 901 |
| Chain | Residue |
| B | THR282 |
| B | GLU284 |
| B | ARG313 |
| B | GLU315 |
| B | TYR326 |
| B | ARG327 |
| B | VAL328 |
| B | PHE331 |
| B | GLU335 |
| B | GLU401 |
| B | VAL402 |
| B | THR403 |
| B | SER404 |
| B | ASN434 |
| B | THR436 |
| B | ALA439 |
| B | HOH905 |
| B | HOH1014 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 12 |
| Details | BINDING: BINDING => ECO:0000269|PubMed:16163389, ECO:0007744|PDB:1WLE |
| Chain | Residue | Details |
| A | THR282 | |
| B | GLU335 | |
| B | GLU401 | |
| B | THR436 | |
| A | ARG313 | |
| A | VAL328 | |
| A | GLU335 | |
| A | GLU401 | |
| A | THR436 | |
| B | THR282 | |
| B | ARG313 | |
| B | VAL328 |
| site_id | SWS_FT_FI2 |
| Number of Residues | 2 |
| Details | MOD_RES: N6-acetyllysine => ECO:0000250|UniProtKB:Q9JJL8 |
| Chain | Residue | Details |
| A | LYS93 | |
| B | LYS93 |
| site_id | SWS_FT_FI3 |
| Number of Residues | 4 |
| Details | MOD_RES: N6-succinyllysine => ECO:0000250|UniProtKB:Q9JJL8 |
| Chain | Residue | Details |
| A | LYS178 | |
| A | LYS320 | |
| B | LYS178 | |
| B | LYS320 |
