1Q2S
Chemical trapping and crystal structure of a catalytic tRNA guanine transglycosylase covalent intermediate
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 401 |
Chain | Residue |
A | CYS318 |
A | CYS320 |
A | CYS323 |
A | HIS349 |
site_id | AC2 |
Number of Residues | 4 |
Details | BINDING SITE FOR RESIDUE ZN B 402 |
Chain | Residue |
B | CYS318 |
B | CYS320 |
B | CYS323 |
B | HIS349 |
site_id | AC3 |
Number of Residues | 4 |
Details | BINDING SITE FOR RESIDUE ZN C 403 |
Chain | Residue |
C | CYS320 |
C | CYS323 |
C | HIS349 |
C | CYS318 |
site_id | AC4 |
Number of Residues | 8 |
Details | BINDING SITE FOR RESIDUE 9DG C 387 |
Chain | Residue |
C | ASP102 |
C | TYR106 |
C | ASP156 |
C | CYS158 |
C | GLY230 |
C | MET260 |
C | GLY261 |
F | N34 |
site_id | AC5 |
Number of Residues | 4 |
Details | BINDING SITE FOR RESIDUE ZN D 404 |
Chain | Residue |
D | CYS318 |
D | CYS320 |
D | CYS323 |
D | HIS349 |
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, ECO:0000305|PubMed:12949492 |
Chain | Residue | Details |
A | SER103 | |
B | SER103 | |
C | SER103 | |
D | SER103 |
site_id | SWS_FT_FI2 |
Number of Residues | 4 |
Details | ACT_SITE: Nucleophile => ECO:0000255|HAMAP-Rule:MF_00168, ECO:0000305|PubMed:12949492 |
Chain | Residue | Details |
A | CYS281 | |
B | CYS281 | |
C | CYS281 | |
D | CYS281 |
site_id | SWS_FT_FI3 |
Number of Residues | 16 |
Details | BINDING: BINDING => ECO:0000255|HAMAP-Rule:MF_00168, ECO:0000269|PubMed:12949492 |
Chain | Residue | Details |
A | SER103 | |
C | GLU157 | |
C | GLY204 | |
C | LEU231 | |
D | SER103 | |
D | GLU157 | |
D | GLY204 | |
D | LEU231 | |
A | GLU157 | |
A | GLY204 | |
A | LEU231 | |
B | SER103 | |
B | GLU157 | |
B | GLY204 | |
B | LEU231 | |
C | SER103 |
site_id | SWS_FT_FI4 |
Number of Residues | 16 |
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 | |
C | ALA321 | |
C | GLN324 | |
C | ASN350 | |
D | HIS319 | |
D | ALA321 | |
D | GLN324 | |
D | ASN350 | |
A | ALA321 | |
A | GLN324 | |
A | ASN350 | |
B | HIS319 | |
B | ALA321 | |
B | GLN324 | |
B | ASN350 | |
C | HIS319 |
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 | CSA2 |
Number of Residues | 1 |
Details | Annotated By Reference To The Literature 1pud |
Chain | Residue | Details |
B | ASP102 |
site_id | CSA3 |
Number of Residues | 1 |
Details | Annotated By Reference To The Literature 1pud |
Chain | Residue | Details |
C | ASP102 |
site_id | CSA4 |
Number of Residues | 1 |
Details | Annotated By Reference To The Literature 1pud |
Chain | Residue | Details |
D | 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 |
site_id | MCSA2 |
Number of Residues | 6 |
Details | M-CSA 881 |
Chain | Residue | Details |
B | SER103 | proton shuttle (general acid/base) |
B | CYS281 | covalent catalysis |
B | HIS319 | metal ligand |
B | ALA321 | metal ligand |
B | GLN324 | metal ligand |
B | ASN350 | metal ligand |
site_id | MCSA3 |
Number of Residues | 6 |
Details | M-CSA 881 |
Chain | Residue | Details |
C | SER103 | proton shuttle (general acid/base) |
C | CYS281 | covalent catalysis |
C | HIS319 | metal ligand |
C | ALA321 | metal ligand |
C | GLN324 | metal ligand |
C | ASN350 | metal ligand |
site_id | MCSA4 |
Number of Residues | 6 |
Details | M-CSA 881 |
Chain | Residue | Details |
D | SER103 | proton shuttle (general acid/base) |
D | CYS281 | covalent catalysis |
D | HIS319 | metal ligand |
D | ALA321 | metal ligand |
D | GLN324 | metal ligand |
D | ASN350 | metal ligand |