3OO0
Structure of apo CheY A113P
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0000156 | molecular_function | phosphorelay response regulator activity |
| A | 0000160 | biological_process | phosphorelay signal transduction system |
| A | 0000287 | molecular_function | magnesium ion binding |
| A | 0005515 | molecular_function | protein binding |
| A | 0005737 | cellular_component | cytoplasm |
| A | 0005829 | cellular_component | cytosol |
| A | 0006935 | biological_process | chemotaxis |
| A | 0007165 | biological_process | signal transduction |
| A | 0009288 | cellular_component | bacterial-type flagellum |
| A | 0009433 | cellular_component | bacterial-type flagellum basal body, C ring |
| A | 0009454 | biological_process | aerotaxis |
| A | 0016407 | molecular_function | acetyltransferase activity |
| A | 0018393 | biological_process | internal peptidyl-lysine acetylation |
| A | 0043052 | biological_process | thermotaxis |
| A | 0046872 | molecular_function | metal ion binding |
| A | 0050920 | biological_process | regulation of chemotaxis |
| A | 0071977 | biological_process | bacterial-type flagellum-dependent swimming motility |
| A | 0097588 | biological_process | archaeal or bacterial-type flagellum-dependent cell motility |
| A | 0120107 | cellular_component | bacterial-type flagellum rotor complex |
| A | 1902021 | biological_process | regulation of bacterial-type flagellum-dependent cell motility |
| B | 0000156 | molecular_function | phosphorelay response regulator activity |
| B | 0000160 | biological_process | phosphorelay signal transduction system |
| B | 0000287 | molecular_function | magnesium ion binding |
| B | 0005515 | molecular_function | protein binding |
| B | 0005737 | cellular_component | cytoplasm |
| B | 0005829 | cellular_component | cytosol |
| B | 0006935 | biological_process | chemotaxis |
| B | 0007165 | biological_process | signal transduction |
| B | 0009288 | cellular_component | bacterial-type flagellum |
| B | 0009433 | cellular_component | bacterial-type flagellum basal body, C ring |
| B | 0009454 | biological_process | aerotaxis |
| B | 0016407 | molecular_function | acetyltransferase activity |
| B | 0018393 | biological_process | internal peptidyl-lysine acetylation |
| B | 0043052 | biological_process | thermotaxis |
| B | 0046872 | molecular_function | metal ion binding |
| B | 0050920 | biological_process | regulation of chemotaxis |
| B | 0071977 | biological_process | bacterial-type flagellum-dependent swimming motility |
| B | 0097588 | biological_process | archaeal or bacterial-type flagellum-dependent cell motility |
| B | 0120107 | cellular_component | bacterial-type flagellum rotor complex |
| B | 1902021 | biological_process | regulation of bacterial-type flagellum-dependent cell motility |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 8 |
| Details | BINDING SITE FOR RESIDUE GOL A 130 |
| Chain | Residue |
| A | LEU46 |
| A | GLY49 |
| A | GLY50 |
| A | TYR51 |
| A | MET78 |
| A | HOH159 |
| A | HOH209 |
| B | ALA77 |
| site_id | AC2 |
| Number of Residues | 7 |
| Details | BINDING SITE FOR RESIDUE GOL A 131 |
| Chain | Residue |
| A | LYS70 |
| A | HOH146 |
| A | HOH240 |
| A | HOH245 |
| A | HOH264 |
| A | HOH280 |
| A | ARG19 |
| site_id | AC3 |
| Number of Residues | 7 |
| Details | BINDING SITE FOR RESIDUE GOL A 132 |
| Chain | Residue |
| A | ASN23 |
| A | MET60 |
| A | ASN62 |
| A | MET63 |
| A | ASP64 |
| A | HOH199 |
| A | HOH271 |
| site_id | AC4 |
| Number of Residues | 10 |
| Details | BINDING SITE FOR RESIDUE GOL A 133 |
| Chain | Residue |
| A | ALA88 |
| A | GLU89 |
| A | ALA90 |
| A | LYS91 |
| A | VAL108 |
| A | LYS109 |
| A | PRO110 |
| A | HOH251 |
| A | HOH269 |
| A | HOH294 |
| site_id | AC5 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE MN A 134 |
| Chain | Residue |
| A | ASP13 |
| A | ASP57 |
| A | ASN59 |
| A | HOH178 |
| A | HOH194 |
| A | SO4401 |
| site_id | AC6 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE NH4 A 135 |
| Chain | Residue |
| A | ASP64 |
| A | HOH153 |
| A | HOH214 |
| A | HOH258 |
| site_id | AC7 |
| Number of Residues | 13 |
| Details | BINDING SITE FOR RESIDUE SO4 A 401 |
| Chain | Residue |
| A | ASP57 |
| A | TRP58 |
| A | ASN59 |
| A | THR87 |
| A | ALA88 |
| A | LYS109 |
| A | MN134 |
| A | HOH164 |
| A | HOH178 |
| A | HOH194 |
| A | HOH206 |
| A | HOH234 |
| B | HOH149 |
| site_id | AC8 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE SO4 A 404 |
| Chain | Residue |
| A | LYS92 |
| A | GLY105 |
| A | TYR106 |
| A | LYS122 |
| A | HOH204 |
| A | HOH272 |
| site_id | AC9 |
| Number of Residues | 8 |
| Details | BINDING SITE FOR RESIDUE GOL B 130 |
| Chain | Residue |
| B | LEU46 |
| B | GLY49 |
| B | GLY50 |
| B | TYR51 |
| B | ALA77 |
| B | LEU81 |
| B | HOH144 |
| B | HOH160 |
| site_id | BC1 |
| Number of Residues | 9 |
| Details | BINDING SITE FOR RESIDUE GOL B 131 |
| Chain | Residue |
| A | ASP3 |
| A | LEU6 |
| B | ARG73 |
| B | ALA74 |
| B | ASP75 |
| B | GLY76 |
| B | SER79 |
| B | HOH150 |
| B | HOH247 |
| site_id | BC2 |
| Number of Residues | 8 |
| Details | BINDING SITE FOR RESIDUE GOL B 132 |
| Chain | Residue |
| A | LYS126 |
| A | LEU127 |
| A | GLY128 |
| B | LYS92 |
| B | SER104 |
| B | LYS126 |
| B | HOH158 |
| B | HOH181 |
| site_id | BC3 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE MN B 133 |
| Chain | Residue |
| B | ASP13 |
| B | ASP57 |
| B | ASN59 |
| B | HOH154 |
| B | HOH179 |
| B | SO4402 |
| site_id | BC4 |
| Number of Residues | 3 |
| Details | BINDING SITE FOR RESIDUE NH4 B 134 |
| Chain | Residue |
| B | ASP64 |
| B | HOH173 |
| B | HOH185 |
| site_id | BC5 |
| Number of Residues | 8 |
| Details | BINDING SITE FOR RESIDUE SO4 B 402 |
| Chain | Residue |
| B | ALA88 |
| B | LYS109 |
| B | MN133 |
| B | HOH154 |
| B | ASP57 |
| B | TRP58 |
| B | ASN59 |
| B | THR87 |
| site_id | BC6 |
| Number of Residues | 8 |
| Details | BINDING SITE FOR RESIDUE SO4 B 403 |
| Chain | Residue |
| B | ASP13 |
| B | PHE14 |
| B | SER15 |
| B | HOH137 |
| B | HOH168 |
| B | HOH222 |
| B | HOH235 |
| B | HOH245 |
| site_id | BC7 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE SO4 B 405 |
| Chain | Residue |
| B | ARG19 |
| B | HOH151 |
| B | HOH189 |
| B | HOH216 |
| B | HOH240 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 234 |
| Details | Domain: {"description":"Response regulatory","evidences":[{"source":"PROSITE-ProRule","id":"PRU00169","evidenceCode":"ECO:0000255"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI2 |
| Number of Residues | 2 |
| Details | Binding site: {"evidences":[{"source":"UniProtKB","id":"A0A0H3AMJ9","evidenceCode":"ECO:0000250"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI3 |
| Number of Residues | 6 |
| Details | Binding site: {"evidences":[{"source":"PubMed","id":"8176739","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"1CHN","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI4 |
| Number of Residues | 2 |
| Details | Modified residue: {"description":"4-aspartylphosphate","evidences":[{"source":"PROSITE-ProRule","id":"PRU00169","evidenceCode":"ECO:0000255"},{"source":"PubMed","id":"1869568","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"2689446","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI5 |
| Number of Residues | 2 |
| Details | Modified residue: {"description":"N6-acetyllysine","evidences":[{"source":"PubMed","id":"11359578","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"9560203","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI6 |
| Number of Residues | 2 |
| Details | Modified residue: {"description":"N6-acetyllysine","evidences":[{"source":"PubMed","id":"1390767","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"9560203","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
