3SP1
Crystal structure of cysteinyl-tRNA synthetase (cysS) from Borrelia burgdorferi
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0000166 | molecular_function | nucleotide binding |
| A | 0004812 | molecular_function | aminoacyl-tRNA ligase activity |
| A | 0004817 | molecular_function | cysteine-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 | 0006423 | biological_process | cysteinyl-tRNA aminoacylation |
| A | 0008270 | molecular_function | zinc ion binding |
| A | 0046872 | molecular_function | metal ion binding |
| B | 0000166 | molecular_function | nucleotide binding |
| B | 0004812 | molecular_function | aminoacyl-tRNA ligase activity |
| B | 0004817 | molecular_function | cysteine-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 | 0006423 | biological_process | cysteinyl-tRNA aminoacylation |
| B | 0008270 | molecular_function | zinc ion binding |
| B | 0046872 | molecular_function | metal ion binding |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE ZN A 481 |
| Chain | Residue |
| A | CYS27 |
| A | CYS221 |
| A | HIS246 |
| A | GLU250 |
| A | HOH525 |
| site_id | AC2 |
| Number of Residues | 11 |
| Details | BINDING SITE FOR RESIDUE AMP A 482 |
| Chain | Residue |
| A | TYR43 |
| A | GLY239 |
| A | ASP241 |
| A | HIS242 |
| A | PHE271 |
| A | LEU272 |
| A | HOH490 |
| A | THR30 |
| A | GLY38 |
| A | ASN39 |
| A | THR42 |
| site_id | AC3 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE ZN B 481 |
| Chain | Residue |
| B | CYS27 |
| B | CYS221 |
| B | HIS246 |
| B | GLU250 |
| B | HOH512 |
| site_id | AC4 |
| Number of Residues | 14 |
| Details | BINDING SITE FOR RESIDUE AMP B 482 |
| Chain | Residue |
| B | THR30 |
| B | HIS36 |
| B | GLY38 |
| B | ASN39 |
| B | THR42 |
| B | TYR43 |
| B | GLY239 |
| B | ASP241 |
| B | HIS242 |
| B | PHE271 |
| B | LEU272 |
| B | LYS278 |
| B | MET279 |
| B | HOH507 |
| site_id | AC5 |
| Number of Residues | 1 |
| Details | BINDING SITE FOR RESIDUE CL B 483 |
| Chain | Residue |
| B | CYS306 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 10 |
| Details | BINDING: BINDING => ECO:0000250 |
| Chain | Residue | Details |
| A | CYS27 | |
| B | LYS281 | |
| A | CYS221 | |
| A | HIS246 | |
| A | GLU250 | |
| A | LYS281 | |
| B | CYS27 | |
| B | CYS221 | |
| B | HIS246 | |
| B | GLU250 |
