5JSW
tRNA guanine Transglycosylase (TGT) in co-crystallized complex with 6-amino-2-((((3a'R,6'R,6a'R)-2,2,2',2'-tetramethyldihydro-3a'H-spiro[[1,3]dioxolane-4,4'-furo[3,4-d][1,3]dioxol]-6'-yl)methyl)amino)-1H-imidazo[4,5-g]quinazolin-8(7H)-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 | queuosine biosynthetic process |
| A | 0016757 | molecular_function | glycosyltransferase activity |
| A | 0016763 | molecular_function | pentosyltransferase activity |
| A | 0046872 | molecular_function | metal ion binding |
| A | 0101030 | biological_process | tRNA-guanine transglycosylation |
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 | 7 |
| Details | binding site for residue EDO A 402 |
| Chain | Residue |
| A | HOH580 |
| A | HOH710 |
| A | SER17 |
| A | ILE18 |
| A | GLU119 |
| A | HOH503 |
| A | HOH566 |
| site_id | AC3 |
| Number of Residues | 4 |
| Details | binding site for residue EDO A 403 |
| Chain | Residue |
| A | ARG38 |
| A | ARG60 |
| A | ALA61 |
| A | GLY63 |
| site_id | AC4 |
| Number of Residues | 6 |
| Details | binding site for residue EDO A 404 |
| Chain | Residue |
| A | HIS145 |
| A | GLY148 |
| A | SER149 |
| A | GLN192 |
| A | HOH603 |
| A | HOH652 |
| site_id | AC5 |
| Number of Residues | 6 |
| Details | binding site for residue EDO A 405 |
| Chain | Residue |
| A | ARG183 |
| A | PHE223 |
| A | ASP224 |
| A | HOH539 |
| A | HOH607 |
| A | HOH700 |
| site_id | AC6 |
| Number of Residues | 8 |
| Details | binding site for residue GOL A 406 |
| Chain | Residue |
| A | PRO56 |
| A | GLU57 |
| A | GLY94 |
| A | TRP95 |
| A | ASP96 |
| A | ARG97 |
| A | LYS325 |
| A | HOH591 |
| site_id | AC7 |
| Number of Residues | 6 |
| Details | binding site for residue GOL A 407 |
| Chain | Residue |
| A | LEU311 |
| A | CYS323 |
| A | LYS325 |
| A | TRP326 |
| A | SER327 |
| A | HOH740 |
| site_id | AC8 |
| Number of Residues | 7 |
| Details | binding site for residue GOL A 408 |
| Chain | Residue |
| A | GLU317 |
| A | LYS360 |
| A | PHE373 |
| A | PHE377 |
| A | ARG380 |
| A | HOH574 |
| A | HOH715 |
| site_id | AC9 |
| Number of Residues | 10 |
| Details | binding site for residue GOL A 409 |
| Chain | Residue |
| A | SER15 |
| A | PHE16 |
| A | GLU119 |
| A | ARG174 |
| A | ARG177 |
| A | ASP254 |
| A | LYS255 |
| A | HOH503 |
| A | HOH580 |
| A | HOH769 |
| site_id | AD1 |
| Number of Residues | 6 |
| Details | binding site for residue GOL A 410 |
| Chain | Residue |
| A | ASN70 |
| A | TYR106 |
| A | GLN107 |
| A | 6MM413 |
| A | HOH545 |
| A | HOH568 |
| site_id | AD2 |
| Number of Residues | 7 |
| Details | binding site for residue GOL A 411 |
| Chain | Residue |
| A | GLN117 |
| A | ARG174 |
| A | PRO252 |
| A | ASP254 |
| A | LYS255 |
| A | HOH520 |
| A | HOH532 |
| site_id | AD3 |
| Number of Residues | 6 |
| Details | binding site for residue GOL A 412 |
| Chain | Residue |
| A | ALA61 |
| A | THR62 |
| A | CYS320 |
| A | ALA321 |
| A | GLU348 |
| A | HOH525 |
| site_id | AD4 |
| Number of Residues | 16 |
| Details | binding site for residue 6MM A 413 |
| 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 | MET260 |
| A | GLY261 |
| A | ARG286 |
| A | GOL410 |
| A | HOH506 |
| site_id | AD5 |
| Number of Residues | 3 |
| Details | binding site for residue CL A 414 |
| Chain | Residue |
| A | THR285 |
| A | ARG289 |
| A | HOH747 |
Functional Information from SwissProt/UniProt
| Chain | Residue | Details |
| A | ASP102 | |
| Chain | Residue | Details |
| A | ASP280 | |
| Chain | Residue | Details |
| A | ASP102 | |
| A | ASP156 | |
| A | GLN203 | |
| A | GLY230 | |
| site_id | SWS_FT_FI4 |
| Number of Residues | 4 |
| Details | BINDING: BINDING => ECO:0000255|HAMAP-Rule:MF_00168, ECO:0000269|PubMed:10413112, ECO:0000269|PubMed:11178905, ECO:0000269|PubMed:11921407, ECO:0000269|PubMed:12646024, ECO:0000269|PubMed:12909636, ECO:0000269|PubMed:12949492, ECO:0000269|PubMed:14523925, ECO:0000269|PubMed:19627989, ECO:0000269|PubMed:8654383, ECO:0000269|PubMed:8961936 |
| Chain | Residue | Details |
| A | CYS318 | |
| A | CYS320 | |
| A | CYS323 | |
| A | HIS349 | |
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 |
