2NQZ
Trna-guanine transglycosylase (TGT) mutant in complex with 7-deaza-7-aminomethyl-guanine
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 |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE ZN A 400 |
| Chain | Residue |
| A | CYS318 |
| A | CYS320 |
| A | CYS323 |
| A | HIS349 |
| site_id | AC2 |
| Number of Residues | 15 |
| Details | BINDING SITE FOR RESIDUE PRF A 500 |
| Chain | Residue |
| A | GLN203 |
| A | GLY229 |
| A | GLY230 |
| A | LEU231 |
| A | SER232 |
| A | MET260 |
| A | GOL704 |
| A | HOH1175 |
| A | HOH1185 |
| A | HOH1282 |
| A | SER103 |
| A | PHE106 |
| A | ASP156 |
| A | VAL158 |
| A | ILE201 |
| site_id | AC3 |
| Number of Residues | 8 |
| Details | BINDING SITE FOR RESIDUE GOL A 700 |
| Chain | Residue |
| A | ALA19 |
| A | THR27 |
| A | GLY28 |
| A | THR39 |
| A | ARG362 |
| A | SER366 |
| A | HOH1206 |
| A | HOH1345 |
| site_id | AC4 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE GOL A 701 |
| Chain | Residue |
| A | PRO56 |
| A | GLU57 |
| A | GLY94 |
| A | TRP95 |
| A | ASP96 |
| A | ARG97 |
| site_id | AC5 |
| Number of Residues | 7 |
| Details | BINDING SITE FOR RESIDUE GOL A 702 |
| Chain | Residue |
| A | GLN117 |
| A | SER118 |
| A | ARG174 |
| A | PRO252 |
| A | ASP254 |
| A | LYS255 |
| A | HOH1161 |
| site_id | AC6 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE GOL A 703 |
| Chain | Residue |
| A | HIS145 |
| A | GLY148 |
| A | SER149 |
| A | GLN192 |
| A | HOH1174 |
| A | HOH1178 |
| site_id | AC7 |
| Number of Residues | 11 |
| Details | BINDING SITE FOR RESIDUE GOL A 704 |
| Chain | Residue |
| A | VAL45 |
| A | ASN70 |
| A | ASP102 |
| A | GLN107 |
| A | GLY261 |
| A | ASP280 |
| A | PRF500 |
| A | HOH1216 |
| A | HOH1306 |
| A | HOH1308 |
| A | HOH1358 |
| site_id | AC8 |
| Number of Residues | 8 |
| Details | BINDING SITE FOR RESIDUE GOL A 705 |
| Chain | Residue |
| A | ALA20 |
| A | ARG21 |
| A | ARG82 |
| A | SER308 |
| A | HIS332 |
| A | ARG336 |
| A | HOH1311 |
| A | HOH1350 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 6 |
| 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 | 4 |
| 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 | 1 |
| 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 | 1 |
| 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 | 7 |
| 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 | 4 |
| 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 | CSA1 |
| Number of Residues | 1 |
| Details | Annotated By Reference To The Literature 1pud |
| Chain | Residue | Details |
| A | ASP102 |
| 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 |
