6H42
crystal structure of the human TGT catalytic subunit QTRT1
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 | 0120507 | cellular_component | tRNA-guanine transglycosylase complex |
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 | 0120507 | cellular_component | tRNA-guanine transglycosylase complex |
B | 1990234 | cellular_component | transferase complex |
Functional Information from PDB Data
site_id | AC1 |
Number of Residues | 5 |
Details | binding site for residue K A 501 |
Chain | Residue |
A | TYR75 |
A | LEU77 |
A | ARG80 |
A | GLY82 |
A | GLU84 |
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 | 2 |
Details | binding site for residue CL A 503 |
Chain | Residue |
A | CYS23 |
A | LYS367 |
site_id | AC4 |
Number of Residues | 2 |
Details | binding site for residue CL A 505 |
Chain | Residue |
A | VAL305 |
A | HOH620 |
site_id | AC5 |
Number of Residues | 4 |
Details | binding site for residue CL A 506 |
Chain | Residue |
A | PHE310 |
A | PHE310 |
A | SER326 |
A | SER326 |
site_id | AC6 |
Number of Residues | 1 |
Details | binding site for residue CL A 507 |
Chain | Residue |
A | CYS280 |
site_id | AC7 |
Number of Residues | 5 |
Details | binding site for residue K B 501 |
Chain | Residue |
B | TYR75 |
B | LEU77 |
B | ARG80 |
B | GLY82 |
B | GLU84 |
site_id | AC8 |
Number of Residues | 4 |
Details | binding site for residue ZN B 502 |
Chain | Residue |
B | CYS317 |
B | CYS319 |
B | CYS322 |
B | HIS348 |
site_id | AC9 |
Number of Residues | 1 |
Details | binding site for residue CL B 503 |
Chain | Residue |
A | ARG327 |
site_id | AD1 |
Number of Residues | 4 |
Details | binding site for residue CL B 504 |
Chain | Residue |
B | CYS23 |
B | LYS367 |
B | ARG368 |
B | PHE369 |
site_id | AD2 |
Number of Residues | 1 |
Details | binding site for residue CL B 506 |
Chain | Residue |
B | CYS280 |
site_id | AD3 |
Number of Residues | 2 |
Details | binding site for residue CL B 507 |
Chain | Residue |
B | PHE310 |
B | SER326 |
site_id | AD4 |
Number of Residues | 1 |
Details | binding site for residue BR B 508 |
Chain | Residue |
B | GLU123 |
site_id | AD5 |
Number of Residues | 2 |
Details | binding site for residue GLU B 509 |
Chain | Residue |
B | ARG184 |
B | HOH601 |
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 | ASP105 | |
B | GLY229 | |
B | CYS317 | |
B | CYS319 | |
B | CYS322 | |
B | HIS348 | |
A | ASP159 | |
A | GLY229 | |
A | CYS317 | |
A | CYS319 | |
A | CYS322 | |
A | HIS348 | |
B | ASP105 | |
B | ASP159 |
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 |