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 400 |
| Chain | Residue |
| A | CYS318 |
| A | CYS320 |
| A | CYS323 |
| A | HIS349 |
| site_id | AC2 |
| Number of Residues | 15 |
| Details | BINDING SITE FOR RESIDUE NEZ A 500 |
| Chain | Residue |
| A | ASP156 |
| A | CYS158 |
| A | ILE201 |
| A | GLN203 |
| A | GLY229 |
| A | GLY230 |
| A | LEU231 |
| A | ALA232 |
| A | MET260 |
| A | GLY261 |
| A | VAL45 |
| A | LEU68 |
| A | ASN70 |
| A | ASP102 |
| A | TYR106 |
| site_id | AC3 |
| Number of Residues | 8 |
| Details | BINDING SITE FOR RESIDUE GOL A 610 |
| Chain | Residue |
| A | PRO56 |
| A | GLU57 |
| A | GLY94 |
| A | TRP95 |
| A | ASP96 |
| A | ARG97 |
| A | HOH1269 |
| A | HOH1309 |
| site_id | AC4 |
| Number of Residues | 7 |
| Details | BINDING SITE FOR RESIDUE GOL A 620 |
| Chain | Residue |
| A | GLU317 |
| A | LYS360 |
| A | PHE373 |
| A | ARG380 |
| A | HOH1052 |
| A | HOH1053 |
| A | HOH1270 |
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 |
