4PDX
Crystal structure of Escherchia coli uncharacterized protein YjcS
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0016787 | molecular_function | hydrolase activity |
| A | 0018741 | molecular_function | linear primary-alkylsulfatase activity |
| A | 0018909 | biological_process | dodecyl sulfate metabolic process |
| A | 0030288 | cellular_component | outer membrane-bounded periplasmic space |
| A | 0042597 | cellular_component | periplasmic space |
| A | 0046872 | molecular_function | metal ion binding |
| A | 0046983 | molecular_function | protein dimerization activity |
| B | 0016787 | molecular_function | hydrolase activity |
| B | 0018741 | molecular_function | linear primary-alkylsulfatase activity |
| B | 0018909 | biological_process | dodecyl sulfate metabolic process |
| B | 0030288 | cellular_component | outer membrane-bounded periplasmic space |
| B | 0042597 | cellular_component | periplasmic space |
| B | 0046872 | molecular_function | metal ion binding |
| B | 0046983 | molecular_function | protein dimerization activity |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 8 |
| Details | binding site for residue SO4 A 701 |
| Chain | Residue |
| A | HIS182 |
| A | HIS317 |
| A | ASN318 |
| A | THR321 |
| A | ARG323 |
| A | ARG328 |
| A | TYR416 |
| A | HOH966 |
| site_id | AC2 |
| Number of Residues | 7 |
| Details | binding site for residue SO4 A 702 |
| Chain | Residue |
| A | LEU402 |
| A | ARG413 |
| A | VAL419 |
| A | HOH1119 |
| A | HOH1169 |
| A | HOH1292 |
| A | LYS401 |
| site_id | AC3 |
| Number of Residues | 9 |
| Details | binding site for residue GOL A 703 |
| Chain | Residue |
| A | GLU512 |
| A | SER513 |
| A | TRP516 |
| A | HOH877 |
| A | HOH902 |
| A | HOH905 |
| A | HOH1126 |
| A | HOH1249 |
| B | HIS442 |
| site_id | AC4 |
| Number of Residues | 9 |
| Details | binding site for residue SO4 B 701 |
| Chain | Residue |
| B | HIS182 |
| B | HIS317 |
| B | ASN318 |
| B | THR321 |
| B | ARG323 |
| B | ARG328 |
| B | TYR416 |
| B | HOH977 |
| B | HOH1038 |
| site_id | AC5 |
| Number of Residues | 9 |
| Details | binding site for residue GOL B 702 |
| Chain | Residue |
| A | HIS442 |
| B | GLU512 |
| B | SER513 |
| B | TRP516 |
| B | HOH884 |
| B | HOH906 |
| B | HOH953 |
| B | HOH1207 |
| B | HOH1246 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 14 |
| Details | BINDING: BINDING => ECO:0000250|UniProtKB:Q9I5I9 |
| Chain | Residue | Details |
| A | HIS180 | |
| B | ASP184 | |
| B | HIS185 | |
| B | GLU291 | |
| B | GLU310 | |
| B | HIS355 | |
| A | HIS182 | |
| A | ASP184 | |
| A | HIS185 | |
| A | GLU291 | |
| A | GLU310 | |
| A | HIS355 | |
| B | HIS180 | |
| B | HIS182 |
| site_id | SWS_FT_FI2 |
| Number of Residues | 6 |
| Details | BINDING: BINDING => ECO:0000269|PubMed:25066955, ECO:0007744|PDB:4PDX |
| Chain | Residue | Details |
| A | ASN318 | |
| A | ARG328 | |
| A | TYR416 | |
| B | ASN318 | |
| B | ARG328 | |
| B | TYR416 |
