6HB5
Crystal structure of E. coli tyrRS in complex with 5'-O-(N-L-tyrosyl)sulfamoyl-cytidine
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0000166 | molecular_function | nucleotide binding |
| A | 0003723 | molecular_function | RNA binding |
| A | 0004812 | molecular_function | aminoacyl-tRNA ligase activity |
| A | 0004831 | molecular_function | tyrosine-tRNA ligase activity |
| A | 0005524 | molecular_function | ATP binding |
| A | 0005737 | cellular_component | cytoplasm |
| A | 0005829 | cellular_component | cytosol |
| A | 0006412 | biological_process | translation |
| A | 0006418 | biological_process | tRNA aminoacylation for protein translation |
| A | 0006437 | biological_process | tyrosyl-tRNA aminoacylation |
| A | 0016020 | cellular_component | membrane |
| A | 0016874 | molecular_function | ligase activity |
| A | 0042803 | molecular_function | protein homodimerization activity |
| A | 0043039 | biological_process | tRNA aminoacylation |
| B | 0000166 | molecular_function | nucleotide binding |
| B | 0003723 | molecular_function | RNA binding |
| B | 0004812 | molecular_function | aminoacyl-tRNA ligase activity |
| B | 0004831 | molecular_function | tyrosine-tRNA ligase activity |
| B | 0005524 | molecular_function | ATP binding |
| B | 0005737 | cellular_component | cytoplasm |
| B | 0005829 | cellular_component | cytosol |
| B | 0006412 | biological_process | translation |
| B | 0006418 | biological_process | tRNA aminoacylation for protein translation |
| B | 0006437 | biological_process | tyrosyl-tRNA aminoacylation |
| B | 0016020 | cellular_component | membrane |
| B | 0016874 | molecular_function | ligase activity |
| B | 0042803 | molecular_function | protein homodimerization activity |
| B | 0043039 | biological_process | tRNA aminoacylation |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 25 |
| Details | binding site for residue YSC A 501 |
| Chain | Residue |
| A | TYR37 |
| A | TYR175 |
| A | GLN179 |
| A | ASP182 |
| A | GLN195 |
| A | GLY197 |
| A | GLY198 |
| A | ASP200 |
| A | GLN201 |
| A | LEU227 |
| A | HOH603 |
| A | GLY39 |
| A | HOH623 |
| A | HOH652 |
| A | HOH700 |
| A | HOH712 |
| A | HOH750 |
| A | HOH832 |
| A | ASP41 |
| A | GLY50 |
| A | HIS51 |
| A | PRO54 |
| A | LEU71 |
| A | THR76 |
| A | ASP81 |
| site_id | AC2 |
| Number of Residues | 2 |
| Details | binding site for residue EDO A 502 |
| Chain | Residue |
| A | PRO33 |
| A | HOH806 |
| site_id | AC3 |
| Number of Residues | 3 |
| Details | binding site for residue EDO A 503 |
| Chain | Residue |
| A | PRO110 |
| A | PHE111 |
| A | LEU310 |
| site_id | AC4 |
| Number of Residues | 7 |
| Details | binding site for residue EDO A 504 |
| Chain | Residue |
| A | ILE386 |
| A | GLU389 |
| A | LYS390 |
| A | GLN391 |
| A | TYR396 |
| A | GLU402 |
| A | HOH612 |
| site_id | AC5 |
| Number of Residues | 4 |
| Details | binding site for residue CL A 505 |
| Chain | Residue |
| A | PHE398 |
| A | ARG403 |
| A | HOH622 |
| A | HOH676 |
| site_id | AC6 |
| Number of Residues | 24 |
| Details | binding site for residue YSC B 501 |
| Chain | Residue |
| B | TYR37 |
| B | GLY39 |
| B | ASP41 |
| B | GLY50 |
| B | HIS51 |
| B | PRO54 |
| B | LEU71 |
| B | THR76 |
| B | ASP81 |
| B | TYR175 |
| B | GLN179 |
| B | ASP182 |
| B | GLN195 |
| B | GLY197 |
| B | GLY198 |
| B | ASP200 |
| B | GLN201 |
| B | LEU227 |
| B | HOH603 |
| B | HOH604 |
| B | HOH620 |
| B | HOH655 |
| B | HOH658 |
| B | HOH683 |
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 | 114 |
| Details | Domain: {"description":"S4 RNA-binding","evidences":[{"source":"PROSITE-ProRule","id":"PRU00182","evidenceCode":"ECO:0000255"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI2 |
| Number of Residues | 18 |
| Details | Motif: {"description":"'HIGH' region","evidences":[{"source":"HAMAP-Rule","id":"MF_02006","evidenceCode":"ECO:0000255"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI3 |
| Number of Residues | 8 |
| Details | Motif: {"description":"'KMSKS' region","evidences":[{"source":"HAMAP-Rule","id":"MF_02006","evidenceCode":"ECO:0000255"}]} |
| 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:0000305"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI5 |
| Number of Residues | 4 |
| 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_FI6 |
| Number of Residues | 2 |
| Details | Binding site: {"evidences":[{"source":"HAMAP-Rule","id":"MF_02006","evidenceCode":"ECO:0000255"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI7 |
| Number of Residues | 4 |
| Details | Site: {"description":"Cross-linked with tRNA by periodate oxidation"} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI8 |
| Number of Residues | 2 |
| Details | Site: {"description":"Cross-linked with tRNA by periodate oxidation; predominant"} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI9 |
| Number of Residues | 2 |
| Details | Modified residue: {"description":"N6-acetyllysine","evidences":[{"source":"PubMed","id":"18723842","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
