1YS6
Crystal structure of the response regulatory protein PrrA from Mycobacterium Tuberculosis
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 CA A 1001 |
Chain | Residue |
A | ASP15 |
A | ASP58 |
A | ASN60 |
A | HOH1058 |
A | HOH1074 |
A | HOH1075 |
site_id | AC2 |
Number of Residues | 6 |
Details | BINDING SITE FOR RESIDUE CA B 1002 |
Chain | Residue |
B | HOH2011 |
B | HOH2064 |
B | HOH2067 |
B | ASP15 |
B | ASP58 |
B | ASN60 |
site_id | AC3 |
Number of Residues | 6 |
Details | BINDING SITE FOR RESIDUE GOL B 2001 |
Chain | Residue |
B | ARG149 |
B | ARG150 |
B | ALA151 |
B | VAL158 |
B | LEU160 |
B | HOH2063 |
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 | ASP15 | |
A | ASP58 | |
A | ASN60 | |
B | ASP15 | |
B | ASP58 | |
B | ASN60 |
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 |