5IUL
Crystal structure of the DesK-DesR complex in the phosphotransfer state with high Mg2+ (150 mM) and BeF3
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0000155 | molecular_function | phosphorelay sensor kinase activity |
| A | 0000160 | biological_process | phosphorelay signal transduction system |
| A | 0016020 | cellular_component | membrane |
| A | 0046983 | molecular_function | protein dimerization activity |
| B | 0000155 | molecular_function | phosphorelay sensor kinase activity |
| B | 0000160 | biological_process | phosphorelay signal transduction system |
| B | 0016020 | cellular_component | membrane |
| B | 0046983 | molecular_function | protein dimerization activity |
| C | 0000160 | biological_process | phosphorelay signal transduction system |
| D | 0000155 | molecular_function | phosphorelay sensor kinase activity |
| D | 0000160 | biological_process | phosphorelay signal transduction system |
| D | 0016020 | cellular_component | membrane |
| D | 0046983 | molecular_function | protein dimerization activity |
| E | 0000155 | molecular_function | phosphorelay sensor kinase activity |
| E | 0000160 | biological_process | phosphorelay signal transduction system |
| E | 0016020 | cellular_component | membrane |
| E | 0046983 | molecular_function | protein dimerization activity |
| F | 0000160 | biological_process | phosphorelay signal transduction system |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 17 |
| Details | binding site for residue ACP A 401 |
| Chain | Residue |
| A | GLU289 |
| A | GLY326 |
| A | HIS335 |
| A | GLY336 |
| A | LEU337 |
| A | THR359 |
| A | MG402 |
| A | HOH502 |
| A | HOH503 |
| A | ASN293 |
| A | LYS296 |
| A | HIS297 |
| A | SER298 |
| A | ASP320 |
| A | THR323 |
| A | PHE324 |
| A | LYS325 |
| site_id | AC2 |
| Number of Residues | 4 |
| Details | binding site for residue MG A 402 |
| Chain | Residue |
| A | GLU289 |
| A | ASN293 |
| A | ACP401 |
| A | HOH502 |
| site_id | AC3 |
| Number of Residues | 17 |
| Details | binding site for residue ACP B 401 |
| Chain | Residue |
| B | GLU289 |
| B | ASN293 |
| B | LYS296 |
| B | HIS297 |
| B | SER298 |
| B | ASP320 |
| B | THR323 |
| B | PHE324 |
| B | LYS325 |
| B | GLY326 |
| B | HIS335 |
| B | GLY336 |
| B | LEU337 |
| B | THR359 |
| B | MG402 |
| B | HOH501 |
| D | LYS312 |
| site_id | AC4 |
| Number of Residues | 4 |
| Details | binding site for residue MG B 402 |
| Chain | Residue |
| B | GLU289 |
| B | ASN293 |
| B | ACP401 |
| B | HOH501 |
| site_id | AC5 |
| Number of Residues | 6 |
| Details | binding site for residue MG C 201 |
| Chain | Residue |
| C | ASP9 |
| C | ASP54 |
| C | GLU56 |
| C | HOH302 |
| C | HOH304 |
| C | HOH306 |
| site_id | AC6 |
| Number of Residues | 3 |
| Details | binding site for residue K C 202 |
| Chain | Residue |
| C | ASN22 |
| C | GLU24 |
| C | MET27 |
| site_id | AC7 |
| Number of Residues | 3 |
| Details | binding site for residue K C 203 |
| Chain | Residue |
| C | LEU69 |
| C | LYS70 |
| C | THR72 |
| site_id | AC8 |
| Number of Residues | 17 |
| Details | binding site for residue ACP D 401 |
| Chain | Residue |
| D | GLU289 |
| D | ASN293 |
| D | LYS296 |
| D | HIS297 |
| D | SER298 |
| D | ASP320 |
| D | THR323 |
| D | PHE324 |
| D | LYS325 |
| D | GLY326 |
| D | HIS335 |
| D | GLY336 |
| D | LEU337 |
| D | THR359 |
| D | MG402 |
| D | HOH501 |
| D | HOH502 |
| site_id | AC9 |
| Number of Residues | 4 |
| Details | binding site for residue MG D 402 |
| Chain | Residue |
| D | GLU289 |
| D | ASN293 |
| D | ACP401 |
| D | HOH501 |
| site_id | AD1 |
| Number of Residues | 17 |
| Details | binding site for residue ACP E 401 |
| Chain | Residue |
| A | LYS312 |
| E | GLU289 |
| E | ASN293 |
| E | LYS296 |
| E | HIS297 |
| E | SER298 |
| E | ASP320 |
| E | THR323 |
| E | PHE324 |
| E | LYS325 |
| E | GLY326 |
| E | HIS335 |
| E | GLY336 |
| E | LEU337 |
| E | THR359 |
| E | MG402 |
| E | HOH501 |
| site_id | AD2 |
| Number of Residues | 4 |
| Details | binding site for residue MG E 402 |
| Chain | Residue |
| E | GLU289 |
| E | ASN293 |
| E | ACP401 |
| E | HOH501 |
| site_id | AD3 |
| Number of Residues | 6 |
| Details | binding site for residue MG F 201 |
| Chain | Residue |
| F | HOH302 |
| F | HOH303 |
| F | HOH304 |
| F | ASP9 |
| F | ASP54 |
| F | GLU56 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 2 |
| Details | MOD_RES: 4-aspartylphosphate => ECO:0000255|PROSITE-ProRule:PRU00169 |
| Chain | Residue | Details |
| C | ASP54 | |
| F | ASP54 | |
| D | GLU188 | |
| E | GLU188 |
