5DGC
Reaction of phosphorylated CheY with imidazole 2 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 | 10 |
Details | binding site for residue BEF A 201 |
Chain | Residue |
A | ASP57 |
A | HOH311 |
A | TRP58 |
A | LYS59 |
A | THR87 |
A | ALA88 |
A | LYS109 |
A | MN202 |
A | IMD203 |
A | IMD204 |
site_id | AC2 |
Number of Residues | 6 |
Details | binding site for residue MN A 202 |
Chain | Residue |
A | ASP13 |
A | ASP57 |
A | LYS59 |
A | BEF201 |
A | IMD203 |
A | HOH311 |
site_id | AC3 |
Number of Residues | 6 |
Details | binding site for residue IMD A 203 |
Chain | Residue |
A | ASP13 |
A | GLN14 |
A | LYS59 |
A | BEF201 |
A | MN202 |
A | IMD204 |
site_id | AC4 |
Number of Residues | 4 |
Details | binding site for residue IMD A 204 |
Chain | Residue |
A | ALA88 |
A | TYR89 |
A | BEF201 |
A | IMD203 |
site_id | AC5 |
Number of Residues | 4 |
Details | binding site for residue IMD A 205 |
Chain | Residue |
A | LYS92 |
A | HOH392 |
B | LYS92 |
B | HOH377 |
site_id | AC6 |
Number of Residues | 4 |
Details | binding site for residue CL A 206 |
Chain | Residue |
A | LYS119 |
A | HOH423 |
B | LYS92 |
B | GLU93 |
site_id | AC7 |
Number of Residues | 5 |
Details | binding site for residue GOL A 207 |
Chain | Residue |
A | LEU46 |
A | GLY49 |
A | GLY50 |
A | TYR51 |
A | ALA77 |
site_id | AC8 |
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 | HOH307 |
site_id | AC9 |
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 | HOH307 |
B | HOH399 |
site_id | AD1 |
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 | AD2 |
Number of Residues | 4 |
Details | binding site for residue IMD B 204 |
Chain | Residue |
B | ALA88 |
B | TYR89 |
B | BEF202 |
B | IMD203 |
site_id | AD3 |
Number of Residues | 5 |
Details | binding site for residue GOL B 205 |
Chain | Residue |
B | ARG19 |
B | LYS70 |
B | HOH306 |
B | HOH317 |
B | HOH341 |
site_id | AD4 |
Number of Residues | 3 |
Details | binding site for residue IMD B 206 |
Chain | Residue |
A | ARG19 |
B | LYS126 |
B | HOH382 |
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 |