6H45
crystal structure of the human TGT catalytic subunit QTRT1 in complex with queuine
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0005515 | molecular_function | protein binding |
| A | 0005634 | cellular_component | nucleus |
| A | 0005737 | cellular_component | cytoplasm |
| A | 0005739 | cellular_component | mitochondrion |
| A | 0005741 | cellular_component | mitochondrial outer membrane |
| A | 0006400 | biological_process | tRNA modification |
| A | 0008033 | biological_process | tRNA processing |
| A | 0008479 | molecular_function | tRNA-guanosine(34) queuine transglycosylase activity |
| A | 0016757 | molecular_function | glycosyltransferase activity |
| A | 0016763 | molecular_function | pentosyltransferase activity |
| A | 0032991 | cellular_component | protein-containing complex |
| A | 0042803 | molecular_function | protein homodimerization activity |
| A | 0046872 | molecular_function | metal ion binding |
| A | 0046982 | molecular_function | protein heterodimerization activity |
| A | 0101030 | biological_process | tRNA-guanine transglycosylation |
| A | 1990234 | cellular_component | transferase complex |
| B | 0005515 | molecular_function | protein binding |
| B | 0005634 | cellular_component | nucleus |
| B | 0005737 | cellular_component | cytoplasm |
| B | 0005739 | cellular_component | mitochondrion |
| B | 0005741 | cellular_component | mitochondrial outer membrane |
| B | 0006400 | biological_process | tRNA modification |
| B | 0008033 | biological_process | tRNA processing |
| B | 0008479 | molecular_function | tRNA-guanosine(34) queuine transglycosylase activity |
| B | 0016757 | molecular_function | glycosyltransferase activity |
| B | 0016763 | molecular_function | pentosyltransferase activity |
| B | 0032991 | cellular_component | protein-containing complex |
| B | 0042803 | molecular_function | protein homodimerization activity |
| B | 0046872 | molecular_function | metal ion binding |
| B | 0046982 | molecular_function | protein heterodimerization activity |
| B | 0101030 | biological_process | tRNA-guanine transglycosylation |
| B | 1990234 | cellular_component | transferase complex |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 13 |
| Details | binding site for residue QEI A 501 |
| Chain | Residue |
| A | PHE109 |
| A | LEU230 |
| A | SER231 |
| A | GLY232 |
| A | MET259 |
| A | ASP159 |
| A | VAL161 |
| A | VAL162 |
| A | SER163 |
| A | SER164 |
| A | ILE200 |
| A | GLY228 |
| A | GLY229 |
| site_id | AC2 |
| Number of Residues | 4 |
| Details | binding site for residue ZN A 502 |
| Chain | Residue |
| A | CYS317 |
| A | CYS319 |
| A | CYS322 |
| A | HIS348 |
| site_id | AC3 |
| Number of Residues | 4 |
| Details | binding site for residue BR A 503 |
| Chain | Residue |
| A | PHE310 |
| A | PHE310 |
| A | SER326 |
| A | SER326 |
| site_id | AC4 |
| Number of Residues | 1 |
| Details | binding site for residue CL A 504 |
| Chain | Residue |
| B | ARG327 |
| site_id | AC5 |
| Number of Residues | 5 |
| Details | binding site for residue K A 506 |
| Chain | Residue |
| A | TYR75 |
| A | LEU77 |
| A | ARG80 |
| A | GLY82 |
| A | GLU84 |
| site_id | AC6 |
| Number of Residues | 1 |
| Details | binding site for residue BR A 507 |
| Chain | Residue |
| A | CYS280 |
| site_id | AC7 |
| Number of Residues | 2 |
| Details | binding site for residue CL B 801 |
| Chain | Residue |
| A | ARG327 |
| B | VAL305 |
| site_id | AC8 |
| Number of Residues | 14 |
| Details | binding site for residue QEI B 802 |
| Chain | Residue |
| B | PHE109 |
| B | ASP159 |
| B | VAL161 |
| B | VAL162 |
| B | SER163 |
| B | SER164 |
| B | ILE200 |
| B | GLY228 |
| B | GLY229 |
| B | LEU230 |
| B | SER231 |
| B | GLY232 |
| B | MET259 |
| B | HOH929 |
| site_id | AC9 |
| Number of Residues | 4 |
| Details | binding site for residue ZN B 803 |
| Chain | Residue |
| B | CYS317 |
| B | CYS319 |
| B | CYS322 |
| B | HIS348 |
| site_id | AD1 |
| Number of Residues | 4 |
| Details | binding site for residue BR B 804 |
| Chain | Residue |
| B | PHE310 |
| B | PHE310 |
| B | SER326 |
| B | SER326 |
| site_id | AD2 |
| Number of Residues | 2 |
| Details | binding site for residue GLU B 805 |
| Chain | Residue |
| B | GLU141 |
| B | ARG184 |
| site_id | AD3 |
| Number of Residues | 1 |
| Details | binding site for residue CL B 807 |
| Chain | Residue |
| B | HOH928 |
| site_id | AD4 |
| Number of Residues | 5 |
| Details | binding site for residue K B 808 |
| Chain | Residue |
| B | TYR75 |
| B | LEU77 |
| B | ARG80 |
| B | GLY82 |
| B | GLU84 |
| site_id | AD5 |
| Number of Residues | 1 |
| Details | binding site for residue BR B 809 |
| Chain | Residue |
| B | CYS280 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 2 |
| Details | ACT_SITE: Proton acceptor => ECO:0000255|HAMAP-Rule:MF_03218 |
| Chain | Residue | Details |
| A | ASP105 | |
| B | ASP105 |
| site_id | SWS_FT_FI2 |
| Number of Residues | 2 |
| Details | ACT_SITE: Nucleophile => ECO:0000255|HAMAP-Rule:MF_03218 |
| Chain | Residue | Details |
| A | ASP279 | |
| B | ASP279 |
| site_id | SWS_FT_FI3 |
| Number of Residues | 14 |
| Details | BINDING: BINDING => ECO:0000255|HAMAP-Rule:MF_03218, ECO:0000269|PubMed:30149595, ECO:0000269|PubMed:34241577, ECO:0007744|PDB:6H45, ECO:0007744|PDB:7NQ4 |
| Chain | Residue | Details |
| A | HIS348 | |
| B | ASP105 | |
| B | ASP159 | |
| B | GLY229 | |
| B | CYS317 | |
| B | CYS319 | |
| B | CYS322 | |
| B | HIS348 | |
| A | ASP105 | |
| A | ASP159 | |
| A | GLY229 | |
| A | CYS317 | |
| A | CYS319 | |
| A | CYS322 |
| site_id | SWS_FT_FI4 |
| Number of Residues | 2 |
| Details | BINDING: BINDING => ECO:0000255|HAMAP-Rule:MF_03218, ECO:0000269|PubMed:34241577, ECO:0007744|PDB:7NQ4 |
| Chain | Residue | Details |
| A | GLN202 | |
| B | GLN202 |
| site_id | SWS_FT_FI5 |
| Number of Residues | 2 |
| Details | MOD_RES: Phosphoserine => ECO:0007744|PubMed:23186163 |
| Chain | Residue | Details |
| A | SER139 | |
| B | SER139 |
