5O8Z
Conformational dynamism for DNA interaction in Salmonella typhimurium RcsB response regulator.
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0000160 | biological_process | phosphorelay signal transduction system |
| A | 0000976 | molecular_function | transcription cis-regulatory region binding |
| A | 0003677 | molecular_function | DNA binding |
| A | 0003700 | molecular_function | DNA-binding transcription factor activity |
| A | 0006351 | biological_process | DNA-templated transcription |
| A | 0006355 | biological_process | regulation of DNA-templated transcription |
| B | 0000160 | biological_process | phosphorelay signal transduction system |
| B | 0000976 | molecular_function | transcription cis-regulatory region binding |
| B | 0003677 | molecular_function | DNA binding |
| B | 0003700 | molecular_function | DNA-binding transcription factor activity |
| B | 0006351 | biological_process | DNA-templated transcription |
| B | 0006355 | biological_process | regulation of DNA-templated transcription |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 10 |
| Details | binding site for residue BEF A 301 |
| Chain | Residue |
| A | ASP56 |
| A | HOH428 |
| A | LEU57 |
| A | SER58 |
| A | THR87 |
| A | MET88 |
| A | LYS109 |
| A | MG302 |
| A | HOH418 |
| A | HOH422 |
| site_id | AC2 |
| Number of Residues | 6 |
| Details | binding site for residue MG A 302 |
| Chain | Residue |
| A | ASP11 |
| A | ASP56 |
| A | SER58 |
| A | BEF301 |
| A | HOH418 |
| A | HOH428 |
| site_id | AC3 |
| Number of Residues | 9 |
| Details | binding site for residue BEF B 301 |
| Chain | Residue |
| B | ASP56 |
| B | LEU57 |
| B | SER58 |
| B | THR87 |
| B | MET88 |
| B | ASN89 |
| B | LYS109 |
| B | MG302 |
| B | HOH420 |
| site_id | AC4 |
| Number of Residues | 6 |
| Details | binding site for residue MG B 302 |
| Chain | Residue |
| B | ASP11 |
| B | ASP56 |
| B | SER58 |
| B | BEF301 |
| B | HOH420 |
| B | HOH432 |
Functional Information from PROSITE/UniProt
| site_id | PS00622 |
| Number of Residues | 28 |
| Details | HTH_LUXR_1 LuxR-type HTH domain signature. GflVteIAkkLnRsikTIssQkkSAmmK |
| Chain | Residue | Details |
| A | GLY165-LYS192 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 238 |
| 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 | 38 |
| Details | DNA binding: {"description":"H-T-H motif","evidences":[{"source":"HAMAP-Rule","id":"MF_00981","evidenceCode":"ECO:0000255"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI3 |
| Number of Residues | 2 |
| Details | Modified residue: {"description":"4-aspartylphosphate","evidences":[{"source":"HAMAP-Rule","id":"MF_00981","evidenceCode":"ECO:0000255"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI4 |
| Number of Residues | 65 |
| Details | Domain: {"description":"HTH luxR-type","evidences":[{"source":"HAMAP-Rule","id":"MF_00981","evidenceCode":"ECO:0000255"}]} |
| Chain | Residue | Details |
