2FXA
Structure of the Protease Production Regulatory Protein hpr from Bacillus subtilis.
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0003677 | molecular_function | DNA binding |
| A | 0003700 | molecular_function | DNA-binding transcription factor activity |
| A | 0005515 | molecular_function | protein binding |
| A | 0006355 | biological_process | regulation of DNA-templated transcription |
| A | 0006950 | biological_process | response to stress |
| A | 0030435 | biological_process | sporulation resulting in formation of a cellular spore |
| A | 0045892 | biological_process | negative regulation of DNA-templated transcription |
| B | 0003677 | molecular_function | DNA binding |
| B | 0003700 | molecular_function | DNA-binding transcription factor activity |
| B | 0005515 | molecular_function | protein binding |
| B | 0006355 | biological_process | regulation of DNA-templated transcription |
| B | 0006950 | biological_process | response to stress |
| B | 0030435 | biological_process | sporulation resulting in formation of a cellular spore |
| B | 0045892 | biological_process | negative regulation of DNA-templated transcription |
| C | 0003677 | molecular_function | DNA binding |
| C | 0003700 | molecular_function | DNA-binding transcription factor activity |
| C | 0005515 | molecular_function | protein binding |
| C | 0006355 | biological_process | regulation of DNA-templated transcription |
| C | 0006950 | biological_process | response to stress |
| C | 0030435 | biological_process | sporulation resulting in formation of a cellular spore |
| C | 0045892 | biological_process | negative regulation of DNA-templated transcription |
| D | 0003677 | molecular_function | DNA binding |
| D | 0003700 | molecular_function | DNA-binding transcription factor activity |
| D | 0005515 | molecular_function | protein binding |
| D | 0006355 | biological_process | regulation of DNA-templated transcription |
| D | 0006950 | biological_process | response to stress |
| D | 0030435 | biological_process | sporulation resulting in formation of a cellular spore |
| D | 0045892 | biological_process | negative regulation of DNA-templated transcription |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE EDO B 206 |
| Chain | Residue |
| A | PHE164 |
| A | SER167 |
| B | VAL15 |
| B | GLN18 |
| B | LYS19 |
| B | HOH347 |
| site_id | AC2 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE EDO A 206 |
| Chain | Residue |
| D | PHE139 |
| A | GLU147 |
| B | PHE139 |
| C | GLU147 |
| site_id | AC3 |
| Number of Residues | 7 |
| Details | BINDING SITE FOR RESIDUE EDO D 206 |
| Chain | Residue |
| C | VAL145 |
| C | GLU147 |
| C | MSE148 |
| D | VAL145 |
| D | GLU147 |
| D | MSE148 |
| D | HOH324 |
| site_id | AC4 |
| Number of Residues | 7 |
| Details | BINDING SITE FOR RESIDUE EDO A 207 |
| Chain | Residue |
| A | VAL145 |
| A | ALA146 |
| A | GLU147 |
| A | MSE148 |
| B | VAL145 |
| B | GLU147 |
| B | MSE148 |
| site_id | AC5 |
| Number of Residues | 3 |
| Details | BINDING SITE FOR RESIDUE EDO B 207 |
| Chain | Residue |
| B | VAL74 |
| B | SER75 |
| B | PHE78 |
| site_id | AC6 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE EDO A 208 |
| Chain | Residue |
| A | GLU144 |
| C | GLU147 |
| D | LYS141 |
| D | GLU144 |
| site_id | AC7 |
| Number of Residues | 3 |
| Details | BINDING SITE FOR RESIDUE EDO B 208 |
| Chain | Residue |
| A | PHE139 |
| B | GLU147 |
| D | GLU147 |
| site_id | AC8 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE EDO C 208 |
| Chain | Residue |
| C | PHE121 |
| C | ASP122 |
| C | ARG125 |
| C | PGE301 |
| site_id | AC9 |
| Number of Residues | 2 |
| Details | BINDING SITE FOR RESIDUE EDO C 209 |
| Chain | Residue |
| C | GLU144 |
| D | LYS19 |
| site_id | BC1 |
| Number of Residues | 7 |
| Details | BINDING SITE FOR RESIDUE EDO D 210 |
| Chain | Residue |
| C | PHE129 |
| C | GLN133 |
| C | TYR136 |
| C | PHE142 |
| D | TYR8 |
| D | ASP9 |
| D | GLU12 |
| site_id | BC2 |
| Number of Residues | 3 |
| Details | BINDING SITE FOR RESIDUE EDO B 211 |
| Chain | Residue |
| A | GLU32 |
| A | EDO212 |
| B | LYS29 |
| site_id | BC3 |
| Number of Residues | 3 |
| Details | BINDING SITE FOR RESIDUE EDO A 212 |
| Chain | Residue |
| A | ASN47 |
| A | HOH313 |
| B | EDO211 |
| site_id | BC4 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE EDO A 213 |
| Chain | Residue |
| A | GLU147 |
| A | HOH305 |
| B | PRO143 |
| B | GLU144 |
| C | GLU144 |
| C | ALA146 |
| site_id | BC5 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE EDO A 214 |
| Chain | Residue |
| A | PRO143 |
| A | GLU144 |
| B | GLU147 |
| D | GLU144 |
| D | ALA146 |
| site_id | BC6 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE PGE C 301 |
| Chain | Residue |
| C | TRP53 |
| C | ASN126 |
| C | EDO208 |
| D | GLN18 |
| D | ALA21 |
| D | GLN22 |
| site_id | BC7 |
| Number of Residues | 10 |
| Details | BINDING SITE FOR RESIDUE P6G B 302 |
| Chain | Residue |
| A | THR17 |
| A | GLN18 |
| A | ALA21 |
| B | TRP35 |
| B | TRP38 |
| B | TRP53 |
| B | GLN57 |
| B | GLU120 |
| B | ASP122 |
| B | ASN126 |
| site_id | BC8 |
| Number of Residues | 10 |
| Details | BINDING SITE FOR RESIDUE 1PE D 303 |
| Chain | Residue |
| C | THR17 |
| C | GLN18 |
| C | ALA21 |
| C | GLN22 |
| D | TRP35 |
| D | TRP38 |
| D | TRP53 |
| D | PHE121 |
| D | ASP122 |
| D | ASN126 |
| site_id | BC9 |
| Number of Residues | 9 |
| Details | BINDING SITE FOR RESIDUE 1PE A 304 |
| Chain | Residue |
| A | TRP35 |
| A | TRP38 |
| A | PHE121 |
| A | ASP122 |
| A | ASN126 |
| A | HOH325 |
| A | HOH349 |
| B | GLN18 |
| B | GLN22 |
Functional Information from PROSITE/UniProt
| site_id | PS01117 |
| Number of Residues | 35 |
| Details | HTH_MARR_1 MarR-type HTH domain signature. TAfNfskk.LEerGYLrfskrlnDKRntyvqlTeeG |
| Chain | Residue | Details |
| A | THR76-GLY110 |
