3OLW
Structural and functional effects of substitution at position T+1 in CheY: CheYA88T-BeF3-Mn complex
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 BEF A 130 |
| Chain | Residue |
| A | ASP57 |
| A | TRP58 |
| A | ASN59 |
| A | THR87 |
| A | THR88 |
| A | LYS109 |
| A | MN131 |
| A | HOH216 |
| site_id | AC2 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE MN A 131 |
| Chain | Residue |
| A | ASP57 |
| A | ASN59 |
| A | BEF130 |
| A | HOH146 |
| A | HOH157 |
| A | ASP13 |
| site_id | AC3 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE GOL A 132 |
| Chain | Residue |
| A | ARG19 |
| A | LYS70 |
| A | HOH182 |
| B | LYS126 |
| B | HOH223 |
| site_id | AC4 |
| Number of Residues | 1 |
| Details | BINDING SITE FOR RESIDUE GOL A 133 |
| Chain | Residue |
| A | LYS7 |
| site_id | AC5 |
| Number of Residues | 3 |
| Details | BINDING SITE FOR RESIDUE GOL A 134 |
| Chain | Residue |
| A | LYS91 |
| A | LYS92 |
| A | GLU93 |
| site_id | AC6 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE GOL A 135 |
| Chain | Residue |
| A | PHE14 |
| A | MET17 |
| A | LYS109 |
| A | HOH157 |
| A | HOH197 |
| A | HOH209 |
| site_id | AC7 |
| Number of Residues | 1 |
| Details | BINDING SITE FOR RESIDUE MN A 136 |
| Chain | Residue |
| A | SER15 |
| site_id | AC8 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE CL A 137 |
| Chain | Residue |
| A | LYS119 |
| B | LYS92 |
| B | GLU93 |
| B | GOL134 |
| B | HOH171 |
| site_id | AC9 |
| Number of Residues | 3 |
| Details | BINDING SITE FOR RESIDUE CL A 138 |
| Chain | Residue |
| A | LYS92 |
| B | LYS92 |
| B | GOL134 |
| site_id | BC1 |
| Number of Residues | 7 |
| Details | BINDING SITE FOR RESIDUE BEF B 130 |
| Chain | Residue |
| B | ASP57 |
| B | TRP58 |
| B | ASN59 |
| B | THR87 |
| B | THR88 |
| B | LYS109 |
| B | MN131 |
| site_id | BC2 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE MN B 131 |
| Chain | Residue |
| B | ASP13 |
| B | ASP57 |
| B | ASN59 |
| B | BEF130 |
| B | HOH147 |
| B | HOH154 |
| site_id | BC3 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE GOL B 132 |
| Chain | Residue |
| B | TRP58 |
| B | ASN59 |
| B | GLU89 |
| B | ASN94 |
| B | HOH220 |
| site_id | BC4 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE GOL B 133 |
| Chain | Residue |
| B | LYS7 |
| B | ASN32 |
| B | GLY50 |
| B | HOH204 |
| site_id | BC5 |
| Number of Residues | 7 |
| Details | BINDING SITE FOR RESIDUE GOL B 134 |
| Chain | Residue |
| A | LYS119 |
| A | CL137 |
| A | CL138 |
| A | HOH210 |
| B | LYS92 |
| B | GLU93 |
| B | HOH224 |
| site_id | BC6 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE GOL B 135 |
| Chain | Residue |
| B | PHE14 |
| B | MET17 |
| B | LYS109 |
| B | HOH221 |
| site_id | BC7 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE SO4 B 136 |
| Chain | Residue |
| B | ARG19 |
| B | HOH180 |
| B | HOH194 |
| B | HOH227 |
| B | HOH241 |
| site_id | BC8 |
| Number of Residues | 1 |
| Details | BINDING SITE FOR RESIDUE MN B 137 |
| Chain | Residue |
| B | SER15 |
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 |
