1WYD
Crystal Structure of Aspartyl-tRNA synthetase from Sulfolobus tokodaii
Functional Information from GO Data
Chain | GOid | namespace | contents |
A | 0000166 | molecular_function | nucleotide binding |
A | 0000287 | molecular_function | magnesium ion binding |
A | 0003676 | molecular_function | nucleic acid binding |
A | 0004812 | molecular_function | aminoacyl-tRNA ligase activity |
A | 0004815 | molecular_function | aspartate-tRNA ligase activity |
A | 0005524 | molecular_function | ATP binding |
A | 0005737 | cellular_component | cytoplasm |
A | 0006412 | biological_process | translation |
A | 0006418 | biological_process | tRNA aminoacylation for protein translation |
A | 0006422 | biological_process | aspartyl-tRNA aminoacylation |
A | 0046872 | molecular_function | metal ion binding |
A | 0050560 | molecular_function | aspartate-tRNA(Asn) ligase activity |
B | 0000166 | molecular_function | nucleotide binding |
B | 0000287 | molecular_function | magnesium ion binding |
B | 0003676 | molecular_function | nucleic acid binding |
B | 0004812 | molecular_function | aminoacyl-tRNA ligase activity |
B | 0004815 | molecular_function | aspartate-tRNA ligase activity |
B | 0005524 | molecular_function | ATP binding |
B | 0005737 | cellular_component | cytoplasm |
B | 0006412 | biological_process | translation |
B | 0006418 | biological_process | tRNA aminoacylation for protein translation |
B | 0006422 | biological_process | aspartyl-tRNA aminoacylation |
B | 0046872 | molecular_function | metal ion binding |
B | 0050560 | molecular_function | aspartate-tRNA(Asn) ligase activity |
Functional Information from PDB Data
site_id | AC1 |
Number of Residues | 4 |
Details | BINDING SITE FOR RESIDUE CL A 431 |
Chain | Residue |
A | THR166 |
A | GLU167 |
A | GLN186 |
A | HOH1038 |
site_id | AC2 |
Number of Residues | 5 |
Details | BINDING SITE FOR RESIDUE SO4 A 1001 |
Chain | Residue |
A | PRO217 |
A | PHE218 |
A | SER413 |
A | VAL414 |
A | LYS415 |
site_id | AC3 |
Number of Residues | 3 |
Details | BINDING SITE FOR RESIDUE CL B 430 |
Chain | Residue |
B | THR166 |
B | GLU167 |
B | GLN186 |
site_id | AC4 |
Number of Residues | 7 |
Details | BINDING SITE FOR RESIDUE SO4 B 1002 |
Chain | Residue |
B | THR216 |
B | PRO217 |
B | PHE218 |
B | SER413 |
B | VAL414 |
B | LYS415 |
B | HOH1152 |
site_id | AC5 |
Number of Residues | 8 |
Details | BINDING SITE FOR RESIDUE EPE A 1003 |
Chain | Residue |
A | PHE218 |
A | HIS219 |
A | LEU220 |
A | PHE223 |
A | ARG403 |
A | VAL414 |
A | HOH1027 |
A | HOH1057 |
site_id | AC6 |
Number of Residues | 6 |
Details | BINDING SITE FOR RESIDUE EPE B 1004 |
Chain | Residue |
B | PHE218 |
B | HIS219 |
B | LEU220 |
B | PHE223 |
B | ARG403 |
B | HOH1046 |
Functional Information from SwissProt/UniProt
site_id | SWS_FT_FI1 |
Number of Residues | 12 |
Details | BINDING: BINDING => ECO:0000255|HAMAP-Rule:MF_02075 |
Chain | Residue | Details |
A | GLU167 | |
B | SER355 | |
B | ARG359 | |
B | GLY400 | |
A | ARG210 | |
A | GLU352 | |
A | SER355 | |
A | ARG359 | |
A | GLY400 | |
B | GLU167 | |
B | ARG210 | |
B | GLU352 |
site_id | SWS_FT_FI2 |
Number of Residues | 2 |
Details | SITE: Important for tRNA non-discrimination => ECO:0000255|HAMAP-Rule:MF_02075 |
Chain | Residue | Details |
A | PRO82 | |
B | PRO82 |
Catalytic Information from CSA
site_id | CSA1 |
Number of Residues | 3 |
Details | Annotated By Reference To The Literature 1asy |
Chain | Residue | Details |
A | ARG403 | |
A | ARG210 | |
A | ASP227 |
site_id | CSA2 |
Number of Residues | 3 |
Details | Annotated By Reference To The Literature 1asy |
Chain | Residue | Details |
B | ARG403 | |
B | ARG210 | |
B | ASP227 |
site_id | CSA3 |
Number of Residues | 1 |
Details | Annotated By Reference To The Literature 1asy |
Chain | Residue | Details |
A | ARG210 |
site_id | CSA4 |
Number of Residues | 1 |
Details | Annotated By Reference To The Literature 1asy |
Chain | Residue | Details |
B | ARG210 |