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 | 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 500 |
Chain | Residue |
A | CYS318 |
A | CYS320 |
A | CYS323 |
A | HIS349 |
site_id | AC2 |
Number of Residues | 6 |
Details | BINDING SITE FOR RESIDUE GOL A 700 |
Chain | Residue |
A | ARG336 |
A | ALA20 |
A | ARG21 |
A | ARG82 |
A | SER308 |
A | HIS332 |
site_id | AC3 |
Number of Residues | 11 |
Details | BINDING SITE FOR RESIDUE GOL A 701 |
Chain | Residue |
A | ALA19 |
A | THR27 |
A | GLY28 |
A | THR29 |
A | SER366 |
A | GOL712 |
A | HOH1072 |
A | HOH1108 |
A | HOH1122 |
A | HOH1148 |
A | HOH1167 |
site_id | AC4 |
Number of Residues | 9 |
Details | BINDING SITE FOR RESIDUE GOL A 702 |
Chain | Residue |
A | PRO56 |
A | GLU57 |
A | GLY94 |
A | TRP95 |
A | ASP96 |
A | ARG97 |
A | HOH1179 |
A | HOH1209 |
A | HOH1272 |
site_id | AC5 |
Number of Residues | 6 |
Details | BINDING SITE FOR RESIDUE GOL A 703 |
Chain | Residue |
A | ASN70 |
A | ASP102 |
A | GLN107 |
A | GLY261 |
A | ASP280 |
A | HOH1160 |
site_id | AC6 |
Number of Residues | 6 |
Details | BINDING SITE FOR RESIDUE GOL A 704 |
Chain | Residue |
A | GLN117 |
A | ARG174 |
A | PRO252 |
A | ASP254 |
A | LYS255 |
A | HOH1051 |
site_id | AC7 |
Number of Residues | 9 |
Details | BINDING SITE FOR RESIDUE GOL A 705 |
Chain | Residue |
A | ARG34 |
A | HIS145 |
A | GLY148 |
A | SER149 |
A | GLU191 |
A | GLN192 |
A | GOL708 |
A | HOH1022 |
A | HOH1079 |
site_id | AC8 |
Number of Residues | 6 |
Details | BINDING SITE FOR RESIDUE GOL A 706 |
Chain | Residue |
A | GLU317 |
A | LYS360 |
A | PHE373 |
A | ARG380 |
A | HOH1025 |
A | HOH1201 |
site_id | AC9 |
Number of Residues | 8 |
Details | BINDING SITE FOR RESIDUE GOL A 707 |
Chain | Residue |
A | MET172 |
A | GLU173 |
A | MET176 |
A | ARG177 |
A | ALA217 |
A | GOL715 |
A | HOH1172 |
A | HOH1181 |
site_id | BC1 |
Number of Residues | 7 |
Details | BINDING SITE FOR RESIDUE GOL A 708 |
Chain | Residue |
A | ARG34 |
A | GLY87 |
A | GLY88 |
A | GLY148 |
A | GOL705 |
A | HOH1046 |
A | HOH1090 |
site_id | BC2 |
Number of Residues | 8 |
Details | BINDING SITE FOR RESIDUE GOL A 709 |
Chain | Residue |
A | GLU81 |
A | GLU138 |
A | ARG139 |
A | GLU142 |
A | HOH1141 |
A | HOH1154 |
A | HOH1217 |
A | HOH1316 |
site_id | BC3 |
Number of Residues | 6 |
Details | BINDING SITE FOR RESIDUE GOL A 711 |
Chain | Residue |
A | CYS158 |
A | GLY229 |
A | GLY230 |
A | LEU231 |
A | ALA232 |
A | HOH1202 |
site_id | BC4 |
Number of Residues | 7 |
Details | BINDING SITE FOR RESIDUE GOL A 712 |
Chain | Residue |
A | ALA19 |
A | ASN304 |
A | ALA305 |
A | ARG306 |
A | SER366 |
A | GOL701 |
A | HOH1148 |
site_id | BC5 |
Number of Residues | 2 |
Details | BINDING SITE FOR RESIDUE GOL A 713 |
Chain | Residue |
A | HOH1004 |
A | HOH1106 |
site_id | BC6 |
Number of Residues | 6 |
Details | BINDING SITE FOR RESIDUE GOL A 715 |
Chain | Residue |
A | GOL707 |
A | HOH1188 |
A | MET176 |
A | ARG177 |
A | ALA217 |
A | ILE221 |
site_id | BC7 |
Number of Residues | 5 |
Details | BINDING SITE FOR RESIDUE GOL A 716 |
Chain | Residue |
A | GLU22 |
A | LYS24 |
A | GLU273 |
A | PHE370 |
A | SER371 |
site_id | BC8 |
Number of Residues | 6 |
Details | BINDING SITE FOR RESIDUE GOL A 717 |
Chain | Residue |
A | PRO249 |
A | MET250 |
A | LEU251 |
A | PRO252 |
A | ASP253 |
A | HOH1276 |
Functional Information from SwissProt/UniProt
Chain | Residue | Details |
A | SER103 | |
Chain | Residue | Details |
A | CYS281 | |
Chain | Residue | Details |
A | SER103 | |
A | GLU157 | |
A | GLY204 | |
A | LEU231 | |
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 | HIS319 | |
A | ALA321 | |
A | GLN324 | |
A | ASN350 | |
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 | SER103 | proton shuttle (general acid/base) |
A | CYS281 | covalent catalysis |
A | HIS319 | metal ligand |
A | ALA321 | metal ligand |
A | GLN324 | metal ligand |
A | ASN350 | metal ligand |