4ZMR
Structural characterization of the full-length response regulator spr1814 in complex with a phosphate analogue reveals a novel conformational plasticity of the linker region
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 | 0000976 | molecular_function | transcription cis-regulatory region binding |
A | 0003677 | molecular_function | DNA binding |
A | 0005829 | cellular_component | cytosol |
A | 0006355 | biological_process | regulation of DNA-templated transcription |
A | 0032993 | cellular_component | protein-DNA complex |
A | 0046872 | molecular_function | metal ion binding |
B | 0000156 | molecular_function | phosphorelay response regulator activity |
B | 0000160 | biological_process | phosphorelay signal transduction system |
B | 0000976 | molecular_function | transcription cis-regulatory region binding |
B | 0003677 | molecular_function | DNA binding |
B | 0005829 | cellular_component | cytosol |
B | 0006355 | biological_process | regulation of DNA-templated transcription |
B | 0032993 | cellular_component | protein-DNA complex |
B | 0046872 | molecular_function | metal ion binding |
Functional Information from PDB Data
site_id | AC1 |
Number of Residues | 6 |
Details | binding site for residue MG A 201 |
Chain | Residue |
A | ASP8 |
A | ASP53 |
A | GLU55 |
A | BEF202 |
A | HOH322 |
A | HOH393 |
site_id | AC2 |
Number of Residues | 11 |
Details | binding site for residue BEF A 202 |
Chain | Residue |
A | THR81 |
A | THR82 |
A | PHE83 |
A | LYS103 |
A | MG201 |
A | HOH322 |
A | HOH393 |
A | HOH409 |
A | ASP53 |
A | VAL54 |
A | GLU55 |
site_id | AC3 |
Number of Residues | 6 |
Details | binding site for residue MG B 201 |
Chain | Residue |
B | ASP8 |
B | ASP53 |
B | GLU55 |
B | BEF202 |
B | HOH325 |
B | HOH389 |
site_id | AC4 |
Number of Residues | 11 |
Details | binding site for residue BEF B 202 |
Chain | Residue |
B | ASP53 |
B | VAL54 |
B | GLU55 |
B | THR81 |
B | THR82 |
B | PHE83 |
B | LYS103 |
B | MG201 |
B | HOH325 |
B | HOH389 |
B | HOH413 |
Functional Information from PROSITE/UniProt
site_id | PS00622 |
Number of Residues | 28 |
Details | HTH_LUXR_1 LuxR-type HTH domain signature. GlsNqeIAdqLyLsngTIrnYvtNIlsK |
Chain | Residue | Details |
A | GLY153-LYS180 |