3FGZ
Crystal Structure of CheY triple mutant F14E, N59M, E89R complexed with BeF3- and Mn2+
Replaces: 2J8EFunctional 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 | 6 |
| Details | BINDING SITE FOR RESIDUE MN A 202 |
| Chain | Residue |
| A | ASP13 |
| A | ASP57 |
| A | MET59 |
| A | BEF130 |
| A | HOH151 |
| A | HOH192 |
| site_id | AC2 |
| Number of Residues | 9 |
| Details | BINDING SITE FOR RESIDUE BEF A 130 |
| Chain | Residue |
| A | THR87 |
| A | ALA88 |
| A | LYS109 |
| A | HOH151 |
| A | HOH156 |
| A | MN202 |
| A | ASP57 |
| A | TRP58 |
| A | MET59 |
| site_id | AC3 |
| Number of Residues | 3 |
| Details | BINDING SITE FOR RESIDUE GOL A 501 |
| Chain | Residue |
| A | ARG19 |
| A | LYS70 |
| B | LYS126 |
| site_id | AC4 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE MN B 202 |
| Chain | Residue |
| B | ASP13 |
| B | ASP57 |
| B | MET59 |
| B | BEF130 |
| B | HOH147 |
| B | HOH178 |
| site_id | AC5 |
| Number of Residues | 8 |
| Details | BINDING SITE FOR RESIDUE BEF B 130 |
| Chain | Residue |
| B | ASP57 |
| B | TRP58 |
| B | MET59 |
| B | THR87 |
| B | ALA88 |
| B | LYS109 |
| B | HOH178 |
| B | MN202 |
| site_id | AC6 |
| Number of Residues | 3 |
| Details | BINDING SITE FOR RESIDUE GOL B 500 |
| Chain | Residue |
| B | ARG19 |
| B | HOH148 |
| B | HOH185 |
| site_id | AC7 |
| Number of Residues | 2 |
| Details | BINDING SITE FOR RESIDUE NH4 B 502 |
| Chain | Residue |
| B | MET17 |
| B | GLN47 |
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:0000269|PubMed:8176739, ECO:0007744|PDB:1CHN |
| Chain | Residue | Details |
| A | ASP13 | |
| A | ASP57 | |
| A | MET59 | |
| B | ASP13 | |
| B | ASP57 | |
| B | MET59 |
| site_id | SWS_FT_FI3 |
| Number of Residues | 2 |
| Details | MOD_RES: 4-aspartylphosphate => ECO:0000255|PROSITE-ProRule:PRU00169, ECO:0000269|PubMed:1869568, ECO:0000269|PubMed:2689446 |
| Chain | Residue | Details |
| A | ASP57 | |
| B | ASP57 |
| site_id | SWS_FT_FI4 |
| Number of Residues | 2 |
| Details | MOD_RES: N6-acetyllysine => ECO:0000269|PubMed:11359578, ECO:0000269|PubMed:9560203 |
| Chain | Residue | Details |
| A | LYS92 | |
| B | LYS92 |
| site_id | SWS_FT_FI5 |
| Number of Residues | 2 |
| Details | MOD_RES: N6-acetyllysine => ECO:0000269|PubMed:1390767, ECO:0000269|PubMed:9560203 |
| Chain | Residue | Details |
| A | LYS109 | |
| B | LYS109 |
