4IF4
Crystal Structure of the Magnesium and beryllofluoride-activated VraR from Staphylococcus aureus
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 | 0005737 | cellular_component | cytoplasm |
| A | 0006355 | biological_process | regulation of DNA-templated transcription |
| A | 0046677 | biological_process | response to antibiotic |
| B | 0000160 | biological_process | phosphorelay signal transduction system |
| B | 0000976 | molecular_function | transcription cis-regulatory region binding |
| B | 0003677 | molecular_function | DNA binding |
| B | 0005737 | cellular_component | cytoplasm |
| B | 0006355 | biological_process | regulation of DNA-templated transcription |
| B | 0046677 | biological_process | response to antibiotic |
| C | 0000160 | biological_process | phosphorelay signal transduction system |
| C | 0000976 | molecular_function | transcription cis-regulatory region binding |
| C | 0003677 | molecular_function | DNA binding |
| C | 0005737 | cellular_component | cytoplasm |
| C | 0006355 | biological_process | regulation of DNA-templated transcription |
| C | 0046677 | biological_process | response to antibiotic |
| D | 0000160 | biological_process | phosphorelay signal transduction system |
| D | 0000976 | molecular_function | transcription cis-regulatory region binding |
| D | 0003677 | molecular_function | DNA binding |
| D | 0005737 | cellular_component | cytoplasm |
| D | 0006355 | biological_process | regulation of DNA-templated transcription |
| D | 0046677 | biological_process | response to antibiotic |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE MG A 300 |
| Chain | Residue |
| A | ASP10 |
| A | ASP55 |
| A | LEU57 |
| A | BEF301 |
| A | HOH427 |
| A | HOH447 |
| site_id | AC2 |
| Number of Residues | 11 |
| Details | BINDING SITE FOR RESIDUE BEF A 301 |
| Chain | Residue |
| A | THR83 |
| A | SER84 |
| A | PHE85 |
| A | LYS105 |
| A | MG300 |
| A | HOH419 |
| A | HOH427 |
| A | HOH447 |
| A | ASP55 |
| A | LEU56 |
| A | LEU57 |
| site_id | AC3 |
| Number of Residues | 2 |
| Details | BINDING SITE FOR RESIDUE SO4 A 302 |
| Chain | Residue |
| A | HIS45 |
| A | LYS48 |
| site_id | AC4 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE MG B 300 |
| Chain | Residue |
| B | ASP10 |
| B | ASP55 |
| B | LEU57 |
| B | BEF301 |
| B | HOH420 |
| B | HOH425 |
| site_id | AC5 |
| Number of Residues | 11 |
| Details | BINDING SITE FOR RESIDUE BEF B 301 |
| Chain | Residue |
| B | ASP55 |
| B | LEU56 |
| B | LEU57 |
| B | THR83 |
| B | SER84 |
| B | PHE85 |
| B | LYS105 |
| B | MG300 |
| B | HOH415 |
| B | HOH420 |
| B | HOH425 |
| site_id | AC6 |
| Number of Residues | 2 |
| Details | BINDING SITE FOR RESIDUE SO4 B 302 |
| Chain | Residue |
| B | HIS45 |
| B | LYS48 |
| site_id | AC7 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE MG C 300 |
| Chain | Residue |
| C | ASP10 |
| C | ASP55 |
| C | LEU57 |
| C | BEF301 |
| C | HOH412 |
| C | HOH418 |
| site_id | AC8 |
| Number of Residues | 10 |
| Details | BINDING SITE FOR RESIDUE BEF C 301 |
| Chain | Residue |
| C | ASP55 |
| C | LEU56 |
| C | LEU57 |
| C | THR83 |
| C | SER84 |
| C | LYS105 |
| C | MG300 |
| C | HOH412 |
| C | HOH418 |
| C | HOH426 |
| site_id | AC9 |
| Number of Residues | 2 |
| Details | BINDING SITE FOR RESIDUE SO4 C 302 |
| Chain | Residue |
| C | HIS45 |
| C | LYS48 |
| site_id | BC1 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE MG D 300 |
| Chain | Residue |
| D | ASP10 |
| D | ASP55 |
| D | LEU57 |
| D | BEF301 |
| D | HOH415 |
| D | HOH426 |
| site_id | BC2 |
| Number of Residues | 10 |
| Details | BINDING SITE FOR RESIDUE BEF D 301 |
| Chain | Residue |
| D | ASP55 |
| D | LEU56 |
| D | LEU57 |
| D | THR83 |
| D | SER84 |
| D | LYS105 |
| D | MG300 |
| D | HOH415 |
| D | HOH424 |
| D | HOH426 |
| site_id | BC3 |
| Number of Residues | 2 |
| Details | BINDING SITE FOR RESIDUE SO4 D 302 |
| Chain | Residue |
| D | HIS45 |
| D | LYS48 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 464 |
| 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 | 260 |
| Details | Domain: {"description":"HTH luxR-type","evidences":[{"source":"PROSITE-ProRule","id":"PRU00411","evidenceCode":"ECO:0000255"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI3 |
| Number of Residues | 76 |
| Details | DNA binding: {"description":"H-T-H motif","evidences":[{"source":"PROSITE-ProRule","id":"PRU00411","evidenceCode":"ECO:0000255"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI4 |
| Number of Residues | 4 |
| Details | Modified residue: {"description":"4-aspartylphosphate","evidences":[{"source":"PROSITE-ProRule","id":"PRU00169","evidenceCode":"ECO:0000255"},{"source":"PubMed","id":"18326495","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
