4L87
Crystal structure of the human seryl-tRNA synthetase in complex with Ser-SA at 2.9 Angstrom resolution
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0000049 | molecular_function | tRNA binding |
| A | 0000122 | biological_process | negative regulation of transcription by RNA polymerase II |
| A | 0000166 | molecular_function | nucleotide binding |
| A | 0000978 | molecular_function | RNA polymerase II cis-regulatory region sequence-specific DNA binding |
| A | 0001514 | biological_process | selenocysteine incorporation |
| A | 0002181 | biological_process | cytoplasmic translation |
| A | 0003677 | molecular_function | DNA binding |
| A | 0004812 | molecular_function | aminoacyl-tRNA ligase activity |
| A | 0004828 | molecular_function | serine-tRNA ligase activity |
| A | 0005515 | molecular_function | protein binding |
| A | 0005524 | molecular_function | ATP binding |
| A | 0005634 | cellular_component | nucleus |
| A | 0005737 | cellular_component | cytoplasm |
| A | 0005829 | cellular_component | cytosol |
| A | 0006400 | biological_process | tRNA modification |
| A | 0006412 | biological_process | translation |
| A | 0006418 | biological_process | tRNA aminoacylation for protein translation |
| A | 0006434 | biological_process | seryl-tRNA aminoacylation |
| A | 0016525 | biological_process | negative regulation of angiogenesis |
| A | 0019899 | molecular_function | enzyme binding |
| A | 0042803 | molecular_function | protein homodimerization activity |
| A | 0060090 | molecular_function | molecular adaptor activity |
| A | 0070062 | cellular_component | extracellular exosome |
| A | 0098619 | molecular_function | selenocysteine-tRNA ligase activity |
| A | 1904046 | biological_process | negative regulation of vascular endothelial growth factor production |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 20 |
| Details | BINDING SITE FOR RESIDUE SSA A 501 |
| Chain | Residue |
| A | THR271 |
| A | GLU325 |
| A | GLU391 |
| A | LEU392 |
| A | VAL393 |
| A | SER394 |
| A | ASN427 |
| A | THR429 |
| A | ALA432 |
| A | THR434 |
| A | ARG435 |
| A | GLU273 |
| A | MG504 |
| A | ARG302 |
| A | GLU304 |
| A | PHE316 |
| A | ARG317 |
| A | VAL318 |
| A | PHE321 |
| A | LYS323 |
| site_id | AC2 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE PO4 A 502 |
| Chain | Residue |
| A | ARG310 |
| A | PHE316 |
| A | ARG317 |
| A | ARG390 |
| A | GLU391 |
| site_id | AC3 |
| Number of Residues | 3 |
| Details | BINDING SITE FOR RESIDUE MG A 503 |
| Chain | Residue |
| A | LYS376 |
| A | ASP378 |
| A | GLU391 |
| site_id | AC4 |
| Number of Residues | 2 |
| Details | BINDING SITE FOR RESIDUE MG A 504 |
| Chain | Residue |
| A | GLU246 |
| A | SSA501 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 4 |
| Details | BINDING: BINDING => ECO:0000269|PubMed:24095058, ECO:0007744|PDB:4L87 |
| Chain | Residue | Details |
| A | THR271 | |
| A | ARG302 | |
| A | GLU325 | |
| A | ASN427 |
| site_id | SWS_FT_FI2 |
| Number of Residues | 2 |
| Details | BINDING: BINDING => ECO:0000269|PubMed:24095058, ECO:0000269|PubMed:26433229, ECO:0007744|PDB:4L87 |
| Chain | Residue | Details |
| A | VAL318 | |
| A | GLU391 |
| site_id | SWS_FT_FI3 |
| Number of Residues | 1 |
| Details | SITE: Important for serine binding => ECO:0000269|PubMed:28236339 |
| Chain | Residue | Details |
| A | THR429 |
| site_id | SWS_FT_FI4 |
| Number of Residues | 1 |
| Details | MOD_RES: Phosphoserine => ECO:0007744|PubMed:17525332 |
| Chain | Residue | Details |
| A | SER241 |
| site_id | SWS_FT_FI5 |
| Number of Residues | 1 |
| Details | MOD_RES: N6-acetyllysine => ECO:0007744|PubMed:19608861 |
| Chain | Residue | Details |
| A | LYS323 |
