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 | 0006351 | biological_process | DNA-templated transcription |
| 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 | 0006351 | biological_process | DNA-templated transcription |
| 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 binding: {"description":"OmpR/PhoB-type","evidences":[{"source":"PROSITE-ProRule","id":"PRU01091","evidenceCode":"ECO:0000255"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI2 |
| Number of Residues | 6 |
| Details | Binding site: {"evidences":[{"source":"PubMed","id":"16434396","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"1YS7","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI3 |
| Number of Residues | 2 |
| Details | Modified residue: {"description":"4-aspartylphosphate","evidences":[{"source":"PROSITE-ProRule","id":"PRU00169","evidenceCode":"ECO:0000255"},{"source":"PubMed","id":"29101285","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI4 |
| Number of Residues | 114 |
| Details | Domain: {"description":"Response regulatory","evidences":[{"source":"PROSITE-ProRule","id":"PRU00169","evidenceCode":"ECO:0000255"}]} |
| Chain | Residue | Details |
