6YIQ
tRNA-Guanine Transglycosylase (TGT) in co-crystallized complex (P2) with 6-amino-2-(methylamino)-4-phenethyl-1,7-dihydro-8H-imidazo[4,5-g]quinazolin-8-one
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0002099 | biological_process | tRNA wobble guanine modification |
| A | 0005737 | cellular_component | cytoplasm |
| A | 0005829 | cellular_component | cytosol |
| A | 0006400 | biological_process | tRNA modification |
| A | 0008033 | biological_process | tRNA processing |
| A | 0008479 | molecular_function | tRNA-guanosine(34) queuine transglycosylase activity |
| A | 0008616 | biological_process | tRNA queuosine(34) biosynthetic process |
| A | 0016740 | molecular_function | transferase activity |
| A | 0016757 | molecular_function | glycosyltransferase activity |
| A | 0046872 | molecular_function | metal ion binding |
| B | 0002099 | biological_process | tRNA wobble guanine modification |
| B | 0005737 | cellular_component | cytoplasm |
| B | 0005829 | cellular_component | cytosol |
| B | 0006400 | biological_process | tRNA modification |
| B | 0008033 | biological_process | tRNA processing |
| B | 0008479 | molecular_function | tRNA-guanosine(34) queuine transglycosylase activity |
| B | 0008616 | biological_process | tRNA queuosine(34) biosynthetic process |
| B | 0016740 | molecular_function | transferase activity |
| B | 0016757 | molecular_function | glycosyltransferase activity |
| B | 0046872 | molecular_function | metal ion binding |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 4 |
| Details | binding site for residue ZN A 401 |
| Chain | Residue |
| A | CYS318 |
| A | CYS320 |
| A | CYS323 |
| A | HIS349 |
| site_id | AC2 |
| Number of Residues | 5 |
| Details | binding site for residue GOL A 402 |
| Chain | Residue |
| A | ALA20 |
| A | ARG21 |
| B | SER308 |
| B | HIS332 |
| B | ARG336 |
| site_id | AC3 |
| Number of Residues | 15 |
| Details | binding site for residue OQN A 403 |
| Chain | Residue |
| A | ASP102 |
| A | SER103 |
| A | TYR106 |
| A | ASP156 |
| A | CYS158 |
| A | ILE201 |
| A | GLN203 |
| A | GLY229 |
| A | GLY230 |
| A | LEU231 |
| A | ALA232 |
| A | TYR258 |
| A | MET260 |
| A | GLY261 |
| A | HOH595 |
| site_id | AC4 |
| Number of Residues | 4 |
| Details | binding site for residue ZN B 401 |
| Chain | Residue |
| B | CYS318 |
| B | CYS320 |
| B | CYS323 |
| B | HIS349 |
| site_id | AC5 |
| Number of Residues | 7 |
| Details | binding site for residue GOL B 402 |
| Chain | Residue |
| B | PRO56 |
| B | GLU57 |
| B | GLY94 |
| B | TRP95 |
| B | ASP96 |
| B | ARG97 |
| B | HOH608 |
| site_id | AC6 |
| Number of Residues | 4 |
| Details | binding site for residue GOL B 403 |
| Chain | Residue |
| B | GLU317 |
| B | LYS360 |
| B | ARG380 |
| B | HOH571 |
| site_id | AC7 |
| Number of Residues | 16 |
| Details | binding site for residue OQN B 404 |
| Chain | Residue |
| B | VAL45 |
| B | ASP102 |
| B | SER103 |
| B | TYR106 |
| B | ASP156 |
| B | CYS158 |
| B | ILE201 |
| B | GLN203 |
| B | GLY229 |
| B | GLY230 |
| B | LEU231 |
| B | ALA232 |
| B | MET260 |
| B | GLY261 |
| B | ASP280 |
| B | HOH552 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 12 |
| Details | Region: {"description":"RNA binding","evidences":[{"source":"HAMAP-Rule","id":"MF_00168","evidenceCode":"ECO:0000255"},{"source":"PubMed","id":"12949492","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI2 |
| Number of Residues | 8 |
| Details | Region: {"description":"RNA binding; important for wobble base 34 recognition","evidences":[{"source":"HAMAP-Rule","id":"MF_00168","evidenceCode":"ECO:0000255"},{"source":"PubMed","id":"12949492","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI3 |
| Number of Residues | 2 |
| Details | Active site: {"description":"Proton acceptor","evidences":[{"source":"HAMAP-Rule","id":"MF_00168","evidenceCode":"ECO:0000255"},{"source":"PubMed","id":"12949492","evidenceCode":"ECO:0000305"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI4 |
| Number of Residues | 2 |
| Details | Active site: {"description":"Nucleophile","evidences":[{"source":"HAMAP-Rule","id":"MF_00168","evidenceCode":"ECO:0000255"},{"source":"PubMed","id":"12949492","evidenceCode":"ECO:0000305"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI5 |
| Number of Residues | 14 |
| Details | Binding site: {"evidences":[{"source":"HAMAP-Rule","id":"MF_00168","evidenceCode":"ECO:0000255"},{"source":"PubMed","id":"12949492","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI6 |
| Number of Residues | 8 |
| Details | Binding site: {"evidences":[{"source":"HAMAP-Rule","id":"MF_00168","evidenceCode":"ECO:0000255"},{"source":"PubMed","id":"10413112","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"11178905","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"11921407","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"12646024","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"12909636","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"12949492","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"14523925","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"19627989","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"8654383","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"8961936","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
Catalytic Information from CSA
| site_id | MCSA1 |
| Number of Residues | 6 |
| Details | M-CSA 881 |
| Chain | Residue | Details |
| A | ASP102 | proton shuttle (general acid/base) |
| A | ASP280 | covalent catalysis |
| A | CYS318 | metal ligand |
| A | CYS320 | metal ligand |
| A | CYS323 | metal ligand |
| A | HIS349 | metal ligand |
| site_id | MCSA2 |
| Number of Residues | 6 |
| Details | M-CSA 881 |
| Chain | Residue | Details |
| B | ASP102 | proton shuttle (general acid/base) |
| B | ASP280 | covalent catalysis |
| B | CYS318 | metal ligand |
| B | CYS320 | metal ligand |
| B | CYS323 | metal ligand |
| B | HIS349 | metal ligand |
