6HDZ
Pseudomonas aeruginosa Seryl-tRNA Synthetase in Complex with 5'-O-(N-(L-seryl)-Sulfamoyl)uridine
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0000166 | molecular_function | nucleotide binding |
| A | 0004812 | molecular_function | aminoacyl-tRNA ligase activity |
| A | 0004828 | molecular_function | serine-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 | 0006434 | biological_process | seryl-tRNA aminoacylation |
| A | 0016260 | biological_process | selenocysteine biosynthetic process |
| B | 0000166 | molecular_function | nucleotide binding |
| B | 0004812 | molecular_function | aminoacyl-tRNA ligase activity |
| B | 0004828 | molecular_function | serine-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 | 0006434 | biological_process | seryl-tRNA aminoacylation |
| B | 0016260 | biological_process | selenocysteine biosynthetic process |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 5 |
| Details | binding site for residue EDO A 501 |
| Chain | Residue |
| A | GLU316 |
| A | ASN401 |
| A | TYR402 |
| A | HOH636 |
| A | HOH689 |
| site_id | AC2 |
| Number of Residues | 9 |
| Details | binding site for residue EDO A 502 |
| Chain | Residue |
| A | ASP284 |
| A | GLY392 |
| A | HOH623 |
| A | HOH631 |
| B | TYR194 |
| A | MET165 |
| A | HIS173 |
| A | MET277 |
| A | PHE283 |
| site_id | AC3 |
| Number of Residues | 5 |
| Details | binding site for residue EDO A 503 |
| Chain | Residue |
| A | GLN209 |
| A | PRO232 |
| A | GLU235 |
| A | FZK504 |
| A | HOH678 |
| site_id | AC4 |
| Number of Residues | 22 |
| Details | binding site for residue FZK A 504 |
| Chain | Residue |
| A | THR233 |
| A | GLU235 |
| A | ARG264 |
| A | ILE278 |
| A | ARG279 |
| A | GLN280 |
| A | PHE283 |
| A | LYS285 |
| A | GLU287 |
| A | GLU351 |
| A | ILE352 |
| A | SER353 |
| A | SER354 |
| A | ASN385 |
| A | SER387 |
| A | ALA390 |
| A | ARG393 |
| A | EDO503 |
| A | NA505 |
| A | HOH603 |
| A | HOH676 |
| A | HOH700 |
| site_id | AC5 |
| Number of Residues | 4 |
| Details | binding site for residue NA A 505 |
| Chain | Residue |
| A | GLU351 |
| A | SER354 |
| A | FZK504 |
| A | HOH787 |
| site_id | AC6 |
| Number of Residues | 4 |
| Details | binding site for residue EDO B 501 |
| Chain | Residue |
| B | GLU316 |
| B | ASN401 |
| B | TYR402 |
| B | HOH618 |
| site_id | AC7 |
| Number of Residues | 3 |
| Details | binding site for residue EDO B 502 |
| Chain | Residue |
| A | TRP126 |
| A | GLY127 |
| B | GLU122 |
| site_id | AC8 |
| Number of Residues | 8 |
| Details | binding site for residue EDO B 503 |
| Chain | Residue |
| A | TYR194 |
| B | HIS173 |
| B | MET277 |
| B | PHE283 |
| B | ASP284 |
| B | GLY392 |
| B | HOH606 |
| B | HOH611 |
| site_id | AC9 |
| Number of Residues | 21 |
| Details | binding site for residue FZK B 504 |
| Chain | Residue |
| B | THR233 |
| B | GLU235 |
| B | ARG264 |
| B | ILE278 |
| B | ARG279 |
| B | GLN280 |
| B | PHE283 |
| B | LYS285 |
| B | GLU287 |
| B | GLU351 |
| B | ILE352 |
| B | SER353 |
| B | SER354 |
| B | ASN385 |
| B | SER387 |
| B | ALA390 |
| B | ARG393 |
| B | NA505 |
| B | HOH651 |
| B | HOH681 |
| B | HOH682 |
| site_id | AD1 |
| Number of Residues | 3 |
| Details | binding site for residue NA B 505 |
| Chain | Residue |
| B | GLU351 |
| B | FZK504 |
| B | HOH706 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 10 |
| Details | BINDING: BINDING => ECO:0000255|HAMAP-Rule:MF_00176 |
| Chain | Residue | Details |
| A | THR233 | |
| B | SER387 | |
| A | ARG264 | |
| A | GLU287 | |
| A | GLU351 | |
| A | SER387 | |
| B | THR233 | |
| B | ARG264 | |
| B | GLU287 | |
| B | GLU351 |
