6I5Y
Crystal structure of E. coli tyrRS in complex with 5'-O-(N-L-tyrosyl)sulfamoyl-adenosine
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 | 28 |
Details | binding site for residue YSA A 501 |
Chain | Residue |
A | TYR37 |
A | ASP81 |
A | TYR175 |
A | GLN179 |
A | ASP182 |
A | GLN195 |
A | GLY197 |
A | GLY198 |
A | ASP200 |
A | GLN201 |
A | PRO226 |
A | GLY39 |
A | LEU227 |
A | ILE228 |
A | HOH601 |
A | HOH630 |
A | HOH641 |
A | HOH642 |
A | HOH651 |
A | HOH701 |
A | HOH844 |
A | ASP41 |
A | GLY50 |
A | HIS51 |
A | VAL53 |
A | PRO54 |
A | LEU71 |
A | THR76 |
site_id | AC2 |
Number of Residues | 5 |
Details | binding site for residue EDO A 502 |
Chain | Residue |
A | PRO110 |
A | PHE111 |
A | LEU310 |
A | VAL311 |
A | HOH615 |
site_id | AC3 |
Number of Residues | 26 |
Details | binding site for residue YSA B 501 |
Chain | Residue |
B | TYR37 |
B | GLY39 |
B | ASP41 |
B | GLY50 |
B | HIS51 |
B | VAL53 |
B | PRO54 |
B | LEU71 |
B | ASP81 |
B | TYR175 |
B | GLN179 |
B | ASP182 |
B | GLN195 |
B | GLY197 |
B | GLY198 |
B | ASP200 |
B | GLN201 |
B | LEU227 |
B | ILE228 |
B | HOH602 |
B | HOH625 |
B | HOH646 |
B | HOH648 |
B | HOH719 |
B | HOH778 |
B | HOH819 |
site_id | AC4 |
Number of Residues | 2 |
Details | binding site for residue EDO B 502 |
Chain | Residue |
B | PRO33 |
B | GLU118 |
site_id | AC5 |
Number of Residues | 7 |
Details | binding site for residue EDO B 503 |
Chain | Residue |
B | ILE386 |
B | GLU389 |
B | LYS390 |
B | GLN391 |
B | TYR396 |
B | GLU402 |
B | HOH693 |
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 | 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_FI4 |
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_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 | 3 |
Details | Site: {"description":"Cross-linked with tRNA by periodate oxidation"} |
Chain | Residue | Details |
site_id | SWS_FT_FI7 |
Number of Residues | 2 |
Details | Site: {"description":"Cross-linked with tRNA by periodate oxidation; predominant"} |
Chain | Residue | Details |
site_id | SWS_FT_FI8 |
Number of Residues | 2 |
Details | Modified residue: {"description":"N6-acetyllysine","evidences":[{"source":"PubMed","id":"18723842","evidenceCode":"ECO:0000269"}]} |
Chain | Residue | Details |