3RVL
Structure of the CheY-BeF3 Complex with substitutions at 59 and 89: N59D and E89R
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 | 10 |
| Details | BINDING SITE FOR RESIDUE BEF A 130 |
| Chain | Residue |
| A | ASP57 |
| A | HOH151 |
| A | TRP58 |
| A | ASP59 |
| A | THR87 |
| A | ALA88 |
| A | LYS109 |
| A | MN131 |
| A | HOH135 |
| A | HOH145 |
| site_id | AC2 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE MN A 131 |
| Chain | Residue |
| A | ASP13 |
| A | ASP57 |
| A | ASP59 |
| A | BEF130 |
| A | HOH135 |
| A | HOH145 |
| site_id | AC3 |
| Number of Residues | 9 |
| Details | BINDING SITE FOR RESIDUE SO4 A 132 |
| Chain | Residue |
| A | ARG19 |
| A | ARG89 |
| A | LYS91 |
| A | ASN94 |
| A | HOH136 |
| A | HOH172 |
| A | HOH235 |
| A | HOH240 |
| A | HOH241 |
| site_id | AC4 |
| Number of Residues | 8 |
| Details | BINDING SITE FOR RESIDUE SO4 A 133 |
| Chain | Residue |
| A | THR16 |
| A | ARG19 |
| A | ARG89 |
| A | HOH172 |
| A | HOH193 |
| A | HOH203 |
| A | HOH314 |
| A | HOH358 |
| site_id | AC5 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE SO4 A 134 |
| Chain | Residue |
| A | LYS91 |
| A | LYS92 |
| A | HOH170 |
| A | HOH212 |
| A | HOH349 |
| A | HOH393 |
| site_id | AC6 |
| Number of Residues | 10 |
| Details | BINDING SITE FOR RESIDUE BEF B 130 |
| Chain | Residue |
| B | ASP57 |
| B | TRP58 |
| B | ASP59 |
| B | THR87 |
| B | ALA88 |
| B | LYS109 |
| B | MN131 |
| B | HOH136 |
| B | HOH143 |
| B | HOH233 |
| site_id | AC7 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE MN B 131 |
| Chain | Residue |
| B | ASP13 |
| B | ASP57 |
| B | ASP59 |
| B | BEF130 |
| B | HOH136 |
| B | HOH143 |
| site_id | AC8 |
| Number of Residues | 3 |
| Details | BINDING SITE FOR RESIDUE MN B 132 |
| Chain | Residue |
| B | ASN62 |
| B | HOH234 |
| B | HOH297 |
| site_id | AC9 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE SO4 B 133 |
| Chain | Residue |
| B | THR16 |
| B | ARG19 |
| B | ARG89 |
| B | HOH178 |
| B | HOH230 |
| B | HOH306 |
| site_id | BC1 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE GOL B 134 |
| Chain | Residue |
| A | LYS119 |
| B | LYS91 |
| B | LYS92 |
| B | GLU93 |
| B | HOH159 |
| B | HOH362 |
| site_id | BC2 |
| Number of Residues | 9 |
| Details | BINDING SITE FOR RESIDUE GOL B 135 |
| Chain | Residue |
| B | LEU46 |
| B | GLY49 |
| B | GLY49 |
| B | GLY50 |
| B | GLY50 |
| B | ALA77 |
| B | MET78 |
| B | HOH165 |
| B | HOH165 |
| site_id | CC1 |
| Number of Residues | 10 |
| Details | ACTIVE SITE FOR RESIDUE BEF A 130 |
| Chain | Residue |
| A | ASP57 |
| A | TRP58 |
| A | ASP59 |
| A | THR87 |
| A | ALA88 |
| A | LYS109 |
| A | MN131 |
| A | HOH135 |
| A | HOH145 |
| A | HOH151 |
| site_id | CC2 |
| Number of Residues | 6 |
| Details | ACTIVE SITE FOR RESIDUE MN A 131 |
| Chain | Residue |
| A | ASP13 |
| A | ASP57 |
| A | ASP59 |
| A | BEF130 |
| A | HOH135 |
| A | HOH145 |
| site_id | CC3 |
| Number of Residues | 10 |
| Details | ACTIVE SITE FOR RESIDUE BEF B 130 |
| Chain | Residue |
| B | ALA88 |
| B | LYS109 |
| B | MN131 |
| B | HOH136 |
| B | HOH143 |
| B | HOH233 |
| B | ASP57 |
| B | TRP58 |
| B | ASP59 |
| B | THR87 |
| site_id | CC4 |
| Number of Residues | 6 |
| Details | ACTIVE SITE FOR RESIDUE MN B 131 |
| Chain | Residue |
| B | ASP13 |
| B | ASP57 |
| B | ASP59 |
| B | BEF130 |
| B | HOH136 |
| B | HOH143 |
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 |
