1SB7
Crystal structure of the E.coli pseudouridine synthase TruD
Functional Information from GO Data
Chain | GOid | namespace | contents |
A | 0001522 | biological_process | pseudouridine synthesis |
A | 0003723 | molecular_function | RNA binding |
A | 0005829 | cellular_component | cytosol |
A | 0006396 | biological_process | RNA processing |
A | 0008033 | biological_process | tRNA processing |
A | 0009451 | biological_process | RNA modification |
A | 0009982 | molecular_function | pseudouridine synthase activity |
A | 0016853 | molecular_function | isomerase activity |
A | 0031119 | biological_process | tRNA pseudouridine synthesis |
A | 0106029 | molecular_function | tRNA pseudouridine synthase activity |
A | 0140098 | molecular_function | catalytic activity, acting on RNA |
A | 0160150 | molecular_function | tRNA pseudouridine(13) synthase activity |
B | 0001522 | biological_process | pseudouridine synthesis |
B | 0003723 | molecular_function | RNA binding |
B | 0005829 | cellular_component | cytosol |
B | 0006396 | biological_process | RNA processing |
B | 0008033 | biological_process | tRNA processing |
B | 0009451 | biological_process | RNA modification |
B | 0009982 | molecular_function | pseudouridine synthase activity |
B | 0016853 | molecular_function | isomerase activity |
B | 0031119 | biological_process | tRNA pseudouridine synthesis |
B | 0106029 | molecular_function | tRNA pseudouridine synthase activity |
B | 0140098 | molecular_function | catalytic activity, acting on RNA |
B | 0160150 | molecular_function | tRNA pseudouridine(13) synthase activity |
Functional Information from PDB Data
site_id | AC1 |
Number of Residues | 5 |
Details | BINDING SITE FOR RESIDUE PO4 B 1301 |
Chain | Residue |
B | LEU126 |
B | ASN129 |
B | ALA326 |
B | GLY327 |
B | HOH1156 |
site_id | AC2 |
Number of Residues | 7 |
Details | BINDING SITE FOR RESIDUE GOL B 1201 |
Chain | Residue |
B | ALA297 |
B | ARG298 |
B | HOH961 |
A | GLY12 |
A | LYS13 |
B | GLY231 |
B | TRP233 |
site_id | AC3 |
Number of Residues | 8 |
Details | BINDING SITE FOR RESIDUE GOL A 1202 |
Chain | Residue |
A | GLY231 |
A | TRP233 |
A | ALA297 |
A | ARG298 |
A | HOH968 |
B | GLY12 |
B | LYS13 |
B | ARG147 |
site_id | AC4 |
Number of Residues | 5 |
Details | BINDING SITE FOR RESIDUE GOL A 1203 |
Chain | Residue |
A | PHE27 |
A | PHE131 |
A | PHE329 |
A | ALA330 |
A | THR331 |
site_id | AC5 |
Number of Residues | 5 |
Details | BINDING SITE FOR RESIDUE GOL B 1204 |
Chain | Residue |
B | ASP32 |
B | LYS127 |
B | GLN306 |
B | GLN307 |
B | HOH1154 |
site_id | AC6 |
Number of Residues | 3 |
Details | BINDING SITE FOR RESIDUE GOL B 1205 |
Chain | Residue |
B | SER309 |
B | TRP310 |
B | HOH1063 |
site_id | AC7 |
Number of Residues | 1 |
Details | BINDING SITE FOR RESIDUE GOL B 1206 |
Chain | Residue |
B | TRP313 |
Functional Information from PROSITE/UniProt
site_id | PS01268 |
Number of Residues | 14 |
Details | UPF0024 Uncharacterized protein family UPF0024 signature. GqKDKhAVTeQwLC |
Chain | Residue | Details |
A | GLY77-CYS90 |
Functional Information from SwissProt/UniProt
site_id | SWS_FT_FI1 |
Number of Residues | 2 |
Details | ACT_SITE: Proton acceptor => ECO:0000255 |
Chain | Residue | Details |
A | GLU31 | |
B | GLU31 |
site_id | SWS_FT_FI2 |
Number of Residues | 2 |
Details | ACT_SITE: Nucleophile => ECO:0000269|PubMed:19664587 |
Chain | Residue | Details |
A | ASP80 | |
B | ASP80 |
site_id | SWS_FT_FI3 |
Number of Residues | 4 |
Details | BINDING: BINDING => ECO:0000250 |
Chain | Residue | Details |
A | PHE27 | |
A | PHE329 | |
B | PHE27 | |
B | PHE329 |
site_id | SWS_FT_FI4 |
Number of Residues | 2 |
Details | BINDING: BINDING => ECO:0000305 |
Chain | Residue | Details |
A | ASN129 | |
B | ASN129 |