1JBE
1.08 A Structure of apo-Chey reveals meta-active conformation
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 |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE SO4 A 301 |
| Chain | Residue |
| A | ASN59 |
| A | LYS109 |
| A | GOL201 |
| A | HOH411 |
| A | HOH416 |
| A | HOH460 |
| site_id | AC2 |
| Number of Residues | 11 |
| Details | BINDING SITE FOR RESIDUE SO4 A 302 |
| Chain | Residue |
| A | TYR106 |
| A | LYS119 |
| A | LYS122 |
| A | HOH424 |
| A | HOH428 |
| A | HOH441 |
| A | HOH448 |
| A | HOH451 |
| A | PRO61 |
| A | ASN62 |
| A | GLY105 |
| site_id | AC3 |
| Number of Residues | 12 |
| Details | BINDING SITE FOR RESIDUE SO4 A 303 |
| Chain | Residue |
| A | ASP13 |
| A | PHE14 |
| A | SER15 |
| A | ALA74 |
| A | SNN75 |
| A | GLY76 |
| A | GLN100 |
| A | GOL202 |
| A | HOH410 |
| A | HOH528 |
| A | HOH549 |
| A | HOH551 |
| site_id | AC4 |
| Number of Residues | 9 |
| Details | BINDING SITE FOR RESIDUE GOL A 201 |
| Chain | Residue |
| A | ASP12 |
| A | PHE14 |
| A | MET17 |
| A | GLN47 |
| A | LYS109 |
| A | SO4301 |
| A | HOH457 |
| A | HOH460 |
| A | HOH537 |
| site_id | AC5 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE GOL A 202 |
| Chain | Residue |
| A | ASP13 |
| A | SER15 |
| A | ARG18 |
| A | GLU37 |
| A | SO4303 |
| A | HOH414 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 1 |
| Details | BINDING: BINDING => ECO:0000250|UniProtKB:A0A0H3AMJ9 |
| Chain | Residue | Details |
| A | ASP12 |
| site_id | SWS_FT_FI2 |
| Number of Residues | 3 |
| Details | BINDING: BINDING => ECO:0000269|PubMed:8176739, ECO:0007744|PDB:1CHN |
| Chain | Residue | Details |
| A | ASP13 | |
| A | ASP57 | |
| A | ASN59 |
| site_id | SWS_FT_FI3 |
| Number of Residues | 1 |
| Details | MOD_RES: 4-aspartylphosphate => ECO:0000255|PROSITE-ProRule:PRU00169, ECO:0000269|PubMed:1869568, ECO:0000269|PubMed:2689446 |
| Chain | Residue | Details |
| A | ASP57 |
| site_id | SWS_FT_FI4 |
| Number of Residues | 1 |
| Details | MOD_RES: N6-acetyllysine => ECO:0000269|PubMed:11359578, ECO:0000269|PubMed:9560203 |
| Chain | Residue | Details |
| A | LYS92 |
| site_id | SWS_FT_FI5 |
| Number of Residues | 1 |
| Details | MOD_RES: N6-acetyllysine => ECO:0000269|PubMed:1390767, ECO:0000269|PubMed:9560203 |
| Chain | Residue | Details |
| A | LYS109 |
