5D2C
Reaction of phosphorylated CheY with imidazole 1 of 3
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 | 0005737 | cellular_component | cytoplasm |
| A | 0006935 | biological_process | chemotaxis |
| A | 0009927 | molecular_function | histidine phosphotransfer kinase activity |
| A | 0046872 | molecular_function | metal ion binding |
| A | 0097588 | biological_process | archaeal or bacterial-type flagellum-dependent cell motility |
| B | 0000155 | molecular_function | phosphorelay sensor kinase activity |
| B | 0000160 | biological_process | phosphorelay signal transduction system |
| B | 0005737 | cellular_component | cytoplasm |
| B | 0006935 | biological_process | chemotaxis |
| B | 0009927 | molecular_function | histidine phosphotransfer kinase activity |
| B | 0046872 | molecular_function | metal ion binding |
| B | 0097588 | biological_process | archaeal or bacterial-type flagellum-dependent cell motility |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 6 |
| Details | binding site for residue MN A 201 |
| Chain | Residue |
| A | ASP13 |
| A | ASP57 |
| A | LYS59 |
| A | BEF202 |
| A | IMD203 |
| A | HOH302 |
| site_id | AC2 |
| Number of Residues | 9 |
| Details | binding site for residue BEF A 202 |
| Chain | Residue |
| A | THR87 |
| A | ALA88 |
| A | LYS109 |
| A | MN201 |
| A | IMD203 |
| A | IMD204 |
| A | ASP57 |
| A | TRP58 |
| A | LYS59 |
| site_id | AC3 |
| Number of Residues | 6 |
| Details | binding site for residue IMD A 203 |
| Chain | Residue |
| A | ASP13 |
| A | GLN14 |
| A | LYS59 |
| A | MN201 |
| A | BEF202 |
| A | IMD204 |
| site_id | AC4 |
| Number of Residues | 4 |
| Details | binding site for residue IMD A 204 |
| Chain | Residue |
| A | ALA88 |
| A | TYR89 |
| A | BEF202 |
| A | IMD203 |
| site_id | AC5 |
| Number of Residues | 4 |
| Details | binding site for residue GOL A 205 |
| Chain | Residue |
| A | ARG19 |
| A | LYS70 |
| A | HOH315 |
| B | LYS126 |
| site_id | AC6 |
| Number of Residues | 6 |
| Details | binding site for residue SO4 A 206 |
| Chain | Residue |
| A | LYS92 |
| A | HOH371 |
| A | HOH372 |
| B | LYS91 |
| B | LYS92 |
| B | HOH329 |
| site_id | AC7 |
| Number of Residues | 4 |
| Details | binding site for residue GOL A 207 |
| Chain | Residue |
| A | LYS91 |
| A | LYS92 |
| A | GLU93 |
| A | HOH359 |
| site_id | AC8 |
| Number of Residues | 7 |
| Details | binding site for residue GOL A 208 |
| Chain | Residue |
| A | LEU46 |
| A | GLY49 |
| A | GLY50 |
| A | TYR51 |
| A | ALA77 |
| A | MET78 |
| A | HOH382 |
| site_id | AC9 |
| Number of Residues | 6 |
| Details | binding site for residue MN B 201 |
| Chain | Residue |
| B | ASP13 |
| B | ASP57 |
| B | LYS59 |
| B | BEF202 |
| B | IMD203 |
| B | HOH306 |
| site_id | AD1 |
| Number of Residues | 11 |
| Details | binding site for residue BEF B 202 |
| Chain | Residue |
| B | ASP57 |
| B | TRP58 |
| B | LYS59 |
| B | THR87 |
| B | ALA88 |
| B | LYS109 |
| B | MN201 |
| B | IMD203 |
| B | IMD204 |
| B | HOH306 |
| B | HOH386 |
| site_id | AD2 |
| Number of Residues | 5 |
| Details | binding site for residue IMD B 203 |
| Chain | Residue |
| B | ASP13 |
| B | LYS59 |
| B | MN201 |
| B | BEF202 |
| B | IMD204 |
| site_id | AD3 |
| Number of Residues | 5 |
| Details | binding site for residue IMD B 204 |
| Chain | Residue |
| B | ALA88 |
| B | TYR89 |
| B | BEF202 |
| B | IMD203 |
| B | HOH386 |
| site_id | AD4 |
| Number of Residues | 4 |
| Details | binding site for residue GOL B 205 |
| Chain | Residue |
| B | ARG19 |
| B | LYS70 |
| B | HOH307 |
| B | HOH367 |
| site_id | AD5 |
| Number of Residues | 7 |
| Details | binding site for residue GOL B 206 |
| Chain | Residue |
| B | SER15 |
| B | ARG18 |
| B | ARG19 |
| B | GLU35 |
| B | HOH303 |
| B | HOH336 |
| B | HOH351 |
| site_id | AD6 |
| Number of Residues | 4 |
| Details | binding site for residue IMD B 207 |
| Chain | Residue |
| B | LEU46 |
| B | GLY49 |
| B | GLY50 |
| B | TYR51 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 2 |
| Details | BINDING: BINDING => ECO:0000250|UniProtKB:A0A0H3AMJ9 |
| Chain | Residue | Details |
| A | ASP12 | |
| B | ASP12 |
| site_id | SWS_FT_FI2 |
| Number of Residues | 6 |
| Details | BINDING: BINDING => ECO:0000250|UniProtKB:P0AE67 |
| Chain | Residue | Details |
| A | LYS59 | |
| B | ASP13 | |
| B | ASP57 | |
| B | LYS59 | |
| A | ASP13 | |
| A | ASP57 |
| site_id | SWS_FT_FI3 |
| Number of Residues | 2 |
| Details | MOD_RES: 4-aspartylphosphate => ECO:0000255|PROSITE-ProRule:PRU00169 |
| Chain | Residue | Details |
| A | ASP57 | |
| B | ASP57 |
| site_id | SWS_FT_FI4 |
| Number of Residues | 4 |
| Details | MOD_RES: N6-acetyllysine => ECO:0000250 |
| Chain | Residue | Details |
| A | LYS92 | |
| A | LYS109 | |
| B | LYS92 | |
| B | LYS109 |
