2ASH
Crystal structure of Queuine tRNA-ribosyltransferase (EC 2.4.2.29) (tRNA-guanine (tm1561) from THERMOTOGA MARITIMA at 1.90 A resolution
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 | 0016763 | molecular_function | pentosyltransferase activity |
| A | 0046872 | molecular_function | metal ion binding |
| A | 0101030 | biological_process | tRNA-guanine transglycosylation |
| B | 0002099 | biological_process | tRNA wobble guanine modification |
| B | 0005737 | cellular_component | cytoplasm |
| B | 0005829 | cellular_component | cytosol |
| 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 |
| C | 0002099 | biological_process | tRNA wobble guanine modification |
| C | 0005737 | cellular_component | cytoplasm |
| C | 0005829 | cellular_component | cytosol |
| C | 0006400 | biological_process | tRNA modification |
| C | 0008033 | biological_process | tRNA processing |
| C | 0008479 | molecular_function | tRNA-guanosine(34) queuine transglycosylase activity |
| C | 0008616 | biological_process | queuosine biosynthetic process |
| C | 0016757 | molecular_function | glycosyltransferase activity |
| C | 0016763 | molecular_function | pentosyltransferase activity |
| C | 0046872 | molecular_function | metal ion binding |
| C | 0101030 | biological_process | tRNA-guanine transglycosylation |
| D | 0002099 | biological_process | tRNA wobble guanine modification |
| D | 0005737 | cellular_component | cytoplasm |
| D | 0005829 | cellular_component | cytosol |
| D | 0006400 | biological_process | tRNA modification |
| D | 0008033 | biological_process | tRNA processing |
| D | 0008479 | molecular_function | tRNA-guanosine(34) queuine transglycosylase activity |
| D | 0008616 | biological_process | queuosine biosynthetic process |
| D | 0016757 | molecular_function | glycosyltransferase activity |
| D | 0016763 | molecular_function | pentosyltransferase activity |
| D | 0046872 | molecular_function | metal ion binding |
| D | 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 | CYS299 |
| A | CYS301 |
| A | CYS304 |
| A | HIS330 |
| site_id | AC2 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE ZN B 400 |
| Chain | Residue |
| B | CYS299 |
| B | CYS301 |
| B | CYS304 |
| B | HIS330 |
| site_id | AC3 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE ZN C 400 |
| Chain | Residue |
| C | CYS301 |
| C | CYS304 |
| C | HIS330 |
| C | CYS299 |
| site_id | AC4 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE ZN D 400 |
| Chain | Residue |
| D | CYS299 |
| D | CYS301 |
| D | CYS304 |
| D | HIS330 |
| site_id | AC5 |
| Number of Residues | 3 |
| Details | BINDING SITE FOR RESIDUE CL D 401 |
| Chain | Residue |
| C | HOH455 |
| D | VAL321 |
| D | HOH510 |
| site_id | AC6 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE CL A 401 |
| Chain | Residue |
| A | VAL321 |
| A | HOH421 |
| A | HOH515 |
| B | HOH529 |
| site_id | AC7 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE CL C 401 |
| Chain | Residue |
| A | ARG309 |
| C | TYR287 |
| C | ARG290 |
| C | SER291 |
| C | HOH495 |
| site_id | AC8 |
| Number of Residues | 7 |
| Details | BINDING SITE FOR RESIDUE CL A 402 |
| Chain | Residue |
| A | TYR287 |
| A | LYS289 |
| A | ARG290 |
| A | SER291 |
| A | HOH553 |
| C | ARG309 |
| C | HOH412 |
| site_id | AC9 |
| Number of Residues | 2 |
| Details | BINDING SITE FOR RESIDUE CL C 402 |
| Chain | Residue |
| C | ARG270 |
| C | HOH433 |
| site_id | BC1 |
| Number of Residues | 3 |
| Details | BINDING SITE FOR RESIDUE EDO C 403 |
| Chain | Residue |
| C | CYS304 |
| C | LYS305 |
| C | PHE307 |
| site_id | BC2 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE EDO D 402 |
| Chain | Residue |
| C | PRO65 |
| D | LYS289 |
| D | SER310 |
| D | HIS313 |
| D | HIS314 |
| D | HOH449 |
| site_id | BC3 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE EDO C 404 |
| Chain | Residue |
| C | SER213 |
| C | ILE214 |
| C | GLY215 |
| C | GLU216 |
| C | ARG218 |
| C | THR221 |
| site_id | BC4 |
| Number of Residues | 7 |
| Details | BINDING SITE FOR RESIDUE EDO C 405 |
| Chain | Residue |
| C | GLU320 |
| C | VAL321 |
| C | LEU322 |
| C | HOH436 |
| C | HOH483 |
| D | LYS39 |
| D | LEU40 |
| site_id | BC5 |
| Number of Residues | 7 |
| Details | BINDING SITE FOR RESIDUE EDO B 401 |
| Chain | Residue |
| A | LYS39 |
| A | LEU40 |
| B | GLU320 |
| B | VAL321 |
| B | LEU322 |
| B | HOH496 |
| B | HOH572 |
| site_id | BC6 |
| Number of Residues | 8 |
| Details | BINDING SITE FOR RESIDUE EDO C 406 |
| Chain | Residue |
| C | CYS144 |
| C | GLY210 |
| C | GLY211 |
| C | LEU212 |
| C | ILE214 |
| C | MET241 |
| C | HOH488 |
| C | HOH524 |
| site_id | BC7 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE EDO A 403 |
| Chain | Residue |
| A | GLU347 |
| C | CYS299 |
| C | GLY300 |
| C | ASN333 |
| C | HOH462 |
| C | HOH529 |
| site_id | BC8 |
| Number of Residues | 8 |
| Details | BINDING SITE FOR RESIDUE EDO A 404 |
| Chain | Residue |
| A | CYS144 |
| A | GLY210 |
| A | GLY211 |
| A | LEU212 |
| A | ILE214 |
| A | MET241 |
| A | HOH483 |
| A | HOH552 |
| site_id | BC9 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE EDO A 405 |
| Chain | Residue |
| A | CYS304 |
| A | LYS305 |
| A | ASN306 |
| A | PHE307 |
| site_id | CC1 |
| Number of Residues | 8 |
| Details | BINDING SITE FOR RESIDUE EDO D 403 |
| Chain | Residue |
| D | HOH562 |
| D | CYS144 |
| D | GLY210 |
| D | GLY211 |
| D | LEU212 |
| D | ILE214 |
| D | MET241 |
| D | HOH473 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 4 |
| Details | ACT_SITE: Proton acceptor => ECO:0000255|HAMAP-Rule:MF_00168 |
| Chain | Residue | Details |
| A | ASP89 | |
| B | ASP89 | |
| C | ASP89 | |
| D | ASP89 |
| site_id | SWS_FT_FI2 |
| Number of Residues | 4 |
| Details | ACT_SITE: Nucleophile => ECO:0000255|HAMAP-Rule:MF_00168 |
| Chain | Residue | Details |
| A | ASP261 | |
| B | ASP261 | |
| C | ASP261 | |
| D | ASP261 |
| site_id | SWS_FT_FI3 |
| Number of Residues | 16 |
| Details | BINDING: BINDING => ECO:0000255|HAMAP-Rule:MF_00168 |
| Chain | Residue | Details |
| A | ASP89 | |
| C | ASP142 | |
| C | GLN184 | |
| C | GLY211 | |
| D | ASP89 | |
| D | ASP142 | |
| D | GLN184 | |
| D | GLY211 | |
| A | ASP142 | |
| A | GLN184 | |
| A | GLY211 | |
| B | ASP89 | |
| B | ASP142 | |
| B | GLN184 | |
| B | GLY211 | |
| C | ASP89 |
| site_id | SWS_FT_FI4 |
| Number of Residues | 16 |
| Details | BINDING: BINDING => ECO:0000255|HAMAP-Rule:MF_00168, ECO:0000269|Ref.2 |
| Chain | Residue | Details |
| A | CYS299 | |
| C | CYS301 | |
| C | CYS304 | |
| C | HIS330 | |
| D | CYS299 | |
| D | CYS301 | |
| D | CYS304 | |
| D | HIS330 | |
| A | CYS301 | |
| A | CYS304 | |
| A | HIS330 | |
| B | CYS299 | |
| B | CYS301 | |
| B | CYS304 | |
| B | HIS330 | |
| C | CYS299 |
Catalytic Information from CSA
| site_id | CSA1 |
| Number of Residues | 1 |
| Details | Annotated By Reference To The Literature 1pud |
| Chain | Residue | Details |
| A | ASP89 |
| site_id | CSA2 |
| Number of Residues | 1 |
| Details | Annotated By Reference To The Literature 1pud |
| Chain | Residue | Details |
| B | ASP89 |
| site_id | CSA3 |
| Number of Residues | 1 |
| Details | Annotated By Reference To The Literature 1pud |
| Chain | Residue | Details |
| C | ASP89 |
| site_id | CSA4 |
| Number of Residues | 1 |
| Details | Annotated By Reference To The Literature 1pud |
| Chain | Residue | Details |
| D | ASP89 |
