1WQ4
Escherichia coli tyrosyl-tRNA synthetase mutant complexed with L-tyrosine
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0000166 | molecular_function | nucleotide binding |
| A | 0004812 | molecular_function | aminoacyl-tRNA ligase activity |
| A | 0004831 | molecular_function | tyrosine-tRNA ligase activity |
| A | 0005524 | molecular_function | ATP binding |
| A | 0006418 | biological_process | tRNA aminoacylation for protein translation |
| A | 0006437 | biological_process | tyrosyl-tRNA aminoacylation |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 14 |
| Details | BINDING SITE FOR RESIDUE TYR A 501 |
| Chain | Residue |
| A | GLY39 |
| A | HOH565 |
| A | HOH584 |
| A | HOH607 |
| A | HOH644 |
| A | HOH701 |
| A | ASP41 |
| A | LEU71 |
| A | ASP81 |
| A | TYR175 |
| A | GLN179 |
| A | ASP182 |
| A | GLN201 |
| A | HOH520 |
Functional Information from PROSITE/UniProt
| site_id | PS00178 |
| Number of Residues | 11 |
| Details | AA_TRNA_LIGASE_I Aminoacyl-transfer RNA synthetases class-I signature. Pt.ADsLHLGHL |
| Chain | Residue | Details |
| A | PRO42-LEU52 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 9 |
| Details | Motif: {"description":"'HIGH' region","evidences":[{"source":"HAMAP-Rule","id":"MF_02006","evidenceCode":"ECO:0000255"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI2 |
| Number of Residues | 4 |
| Details | Motif: {"description":"'KMSKS' region","evidences":[{"source":"HAMAP-Rule","id":"MF_02006","evidenceCode":"ECO:0000255"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI3 |
| Number of Residues | 1 |
| Details | Binding site: {"evidences":[{"source":"HAMAP-Rule","id":"MF_02006","evidenceCode":"ECO:0000255"},{"source":"PubMed","id":"15663931","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"15671170","evidenceCode":"ECO:0000305"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI4 |
| Number of Residues | 2 |
| Details | Binding site: {"evidences":[{"source":"HAMAP-Rule","id":"MF_02006","evidenceCode":"ECO:0000255"},{"source":"PubMed","id":"15663931","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"15671170","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"20159998","evidenceCode":"ECO:0000305"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI5 |
| Number of Residues | 1 |
| Details | Binding site: {"evidences":[{"source":"HAMAP-Rule","id":"MF_02006","evidenceCode":"ECO:0000255"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI6 |
| Number of Residues | 2 |
| Details | Site: {"description":"Cross-linked with tRNA by periodate oxidation"} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI7 |
| Number of Residues | 1 |
| Details | Site: {"description":"Cross-linked with tRNA by periodate oxidation; predominant"} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI8 |
| Number of Residues | 1 |
| Details | Modified residue: {"description":"N6-acetyllysine","evidences":[{"source":"PubMed","id":"18723842","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
Catalytic Information from CSA
| site_id | CSA1 |
| Number of Residues | 2 |
| Details | Annotated By Reference To The Literature 1d2r |
| Chain | Residue | Details |
| A | LYS238 | |
| A | LYS235 |
| site_id | CSA2 |
| Number of Residues | 4 |
| Details | Annotated By Reference To The Literature 1d2r |
| Chain | Residue | Details |
| A | LYS85 | |
| A | LYS238 | |
| A | LYS235 | |
| A | ARG89 |
