5LPT
tRNA guanine Transglycosylase (TGT) in co-crystallized complex (space group P21) with 6-amino-2-(methylamino)-4-(2-((2R,3R,4S,5R,6S)-3,4,5,6-tetramethoxytetrahydro-2H-pyran-2-yl)ethyl)-1H-imidazo[4,5-g]quinazolin-8(7H)-one
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| 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 |
| 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 | queuosine biosynthetic process |
| B | 0016757 | molecular_function | glycosyltransferase activity |
| B | 0016763 | molecular_function | pentosyltransferase activity |
| B | 0046872 | molecular_function | metal ion binding |
| B | 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 | 21 |
| Details | binding site for residue 726 A 402 |
| Chain | Residue |
| A | TYR106 |
| A | GLN107 |
| A | ASP156 |
| A | CYS158 |
| A | GLN203 |
| A | GLY229 |
| A | GLY230 |
| A | LEU231 |
| A | ALA232 |
| A | TYR258 |
| A | MET260 |
| A | GLY261 |
| A | ASP280 |
| A | VAL282 |
| A | HOH543 |
| B | HOH556 |
| A | LEU68 |
| A | GLY69 |
| A | ASN70 |
| A | ASP102 |
| A | SER103 |
| site_id | AC3 |
| Number of Residues | 7 |
| Details | binding site for residue GOL A 403 |
| Chain | Residue |
| A | GLY46 |
| A | GLY69 |
| A | ASN70 |
| A | LEU74 |
| A | MET93 |
| A | HOH505 |
| A | HOH585 |
| 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 | 21 |
| Details | binding site for residue 726 B 402 |
| Chain | Residue |
| A | GLU339 |
| A | HOH554 |
| B | GLY69 |
| B | ASN70 |
| B | ASP102 |
| B | SER103 |
| B | TYR106 |
| B | GLN107 |
| B | ASP156 |
| B | CYS158 |
| B | ILE201 |
| B | GLN203 |
| B | GLY229 |
| B | GLY230 |
| B | LEU231 |
| B | ALA232 |
| B | TYR258 |
| B | MET260 |
| B | GLY261 |
| B | ASP280 |
| B | HOH512 |
| site_id | AC6 |
| Number of Residues | 4 |
| Details | binding site for residue GOL B 403 |
| Chain | Residue |
| B | LYS360 |
| B | ARG380 |
| B | HOH525 |
| B | HOH526 |
| site_id | AC7 |
| Number of Residues | 5 |
| Details | binding site for residue GOL B 404 |
| Chain | Residue |
| B | ALA20 |
| B | ARG21 |
| B | ILE365 |
| B | SER366 |
| B | GLY368 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 2 |
| Details | ACT_SITE: Proton acceptor => ECO:0000255|HAMAP-Rule:MF_00168, ECO:0000305|PubMed:12949492 |
| Chain | Residue | Details |
| A | ASP102 | |
| B | ASP102 |
| site_id | SWS_FT_FI2 |
| Number of Residues | 2 |
| Details | ACT_SITE: Nucleophile => ECO:0000255|HAMAP-Rule:MF_00168, ECO:0000305|PubMed:12949492 |
| Chain | Residue | Details |
| A | ASP280 | |
| B | ASP280 |
| site_id | SWS_FT_FI3 |
| Number of Residues | 8 |
| Details | BINDING: BINDING => ECO:0000255|HAMAP-Rule:MF_00168, ECO:0000269|PubMed:12949492 |
| Chain | Residue | Details |
| A | ASP102 | |
| A | ASP156 | |
| A | GLN203 | |
| A | GLY230 | |
| B | ASP102 | |
| B | ASP156 | |
| B | GLN203 | |
| B | GLY230 |
| site_id | SWS_FT_FI4 |
| Number of Residues | 8 |
| 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 | |
| B | CYS318 | |
| B | CYS320 | |
| B | CYS323 | |
| B | 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 |
| 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 |
