1YS7
Crystal structure of the response regulator protein prrA complexed with Mg2+
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 | 0000976 | molecular_function | transcription cis-regulatory region binding |
A | 0003677 | molecular_function | DNA binding |
A | 0005509 | molecular_function | calcium ion binding |
A | 0005737 | cellular_component | cytoplasm |
A | 0005829 | cellular_component | cytosol |
A | 0005886 | cellular_component | plasma membrane |
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 | 0000287 | molecular_function | magnesium ion binding |
B | 0000976 | molecular_function | transcription cis-regulatory region binding |
B | 0003677 | molecular_function | DNA binding |
B | 0005509 | molecular_function | calcium ion binding |
B | 0005737 | cellular_component | cytoplasm |
B | 0005829 | cellular_component | cytosol |
B | 0005886 | cellular_component | plasma membrane |
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 B 1001 |
Chain | Residue |
B | ASP15 |
B | ASP58 |
B | ASN60 |
B | HOH3006 |
B | HOH3013 |
B | HOH3028 |
site_id | AC2 |
Number of Residues | 6 |
Details | BINDING SITE FOR RESIDUE MG A 1002 |
Chain | Residue |
A | HOH4014 |
A | HOH4021 |
A | HOH4037 |
A | ASP15 |
A | ASP58 |
A | ASN60 |
site_id | AC3 |
Number of Residues | 4 |
Details | BINDING SITE FOR RESIDUE ACT A 4001 |
Chain | Residue |
A | TYR105 |
A | LEU106 |
A | VAL107 |
A | ARG118 |
site_id | AC4 |
Number of Residues | 6 |
Details | BINDING SITE FOR RESIDUE ACT A 4002 |
Chain | Residue |
A | ARG181 |
A | ARG224 |
A | GLY225 |
A | PHE228 |
A | HOH4030 |
A | HOH4044 |
site_id | AC5 |
Number of Residues | 4 |
Details | BINDING SITE FOR RESIDUE TRS B 3001 |
Chain | Residue |
B | GLU49 |
B | ARG94 |
B | TYR105 |
B | ASN198 |
site_id | AC6 |
Number of Residues | 8 |
Details | BINDING SITE FOR RESIDUE GOL B 2001 |
Chain | Residue |
B | ARG149 |
B | ARG150 |
B | ALA151 |
B | VAL158 |
B | ASP159 |
B | LEU160 |
B | PHE165 |
B | HOH3033 |
site_id | AC7 |
Number of Residues | 8 |
Details | BINDING SITE FOR RESIDUE GOL B 2002 |
Chain | Residue |
A | ASP18 |
A | GLU135 |
B | ASP15 |
B | ASP16 |
B | SER17 |
B | HOH3017 |
B | HOH3021 |
B | HOH3052 |
Functional Information from SwissProt/UniProt
site_id | SWS_FT_FI1 |
Number of Residues | 196 |
Details | DNA_BIND: OmpR/PhoB-type => ECO:0000255|PROSITE-ProRule:PRU01091 |
Chain | Residue | Details |
A | SER134-MET232 | |
B | SER134-MET232 |
site_id | SWS_FT_FI2 |
Number of Residues | 6 |
Details | BINDING: BINDING => ECO:0000269|PubMed:16434396, ECO:0007744|PDB:1YS7 |
Chain | Residue | Details |
A | ASN60 | |
A | ASP15 | |
A | ASP58 | |
B | ASP58 | |
B | ASN60 | |
B | ASP15 |
site_id | SWS_FT_FI3 |
Number of Residues | 2 |
Details | MOD_RES: Phosphothreonine => ECO:0000269|PubMed:29101285 |
Chain | Residue | Details |
A | THR6 | |
B | THR6 |
site_id | SWS_FT_FI4 |
Number of Residues | 2 |
Details | MOD_RES: 4-aspartylphosphate => ECO:0000255|PROSITE-ProRule:PRU00169, ECO:0000269|PubMed:29101285 |
Chain | Residue | Details |
A | ASP58 | |
B | ASP58 |