3CHY
CRYSTAL STRUCTURE OF ESCHERICHIA COLI CHEY REFINED AT 1.7-ANGSTROM RESOLUTION
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 | 7 |
Details | BINDING SITE FOR RESIDUE SO4 A 401 |
Chain | Residue |
A | PHE14 |
A | ASN59 |
A | LYS109 |
A | HOH202 |
A | HOH203 |
A | HOH261 |
A | HOH305 |
site_id | AC2 |
Number of Residues | 11 |
Details | BINDING SITE FOR RESIDUE SO4 A 402 |
Chain | Residue |
A | GLY105 |
A | TYR106 |
A | LYS119 |
A | LYS122 |
A | HOH218 |
A | HOH234 |
A | HOH254 |
A | HOH258 |
A | HOH293 |
A | PRO61 |
A | ASN62 |
site_id | AC3 |
Number of Residues | 5 |
Details | BINDING SITE FOR RESIDUE SO4 A 403 |
Chain | Residue |
A | ASP13 |
A | SER15 |
A | GLY76 |
A | GLN100 |
A | HOH213 |
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 | ASP13 |
site_id | SWS_FT_FI2 |
Number of Residues | 3 |
Details | BINDING: BINDING => ECO:0000269|PubMed:8176739, ECO:0007744|PDB:1CHN |
Chain | Residue | Details |
A | PHE14 | |
A | TRP58 | |
A | MET60 |
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 | TRP58 |
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 | GLU93 |
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 | PRO110 |