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 |
Functional Information from SwissProt/UniProt
site_id | SWS_FT_FI1 |
Number of Residues | 92 |
Details | DNA_BIND: H-T-H motif => ECO:0000255|HAMAP-Rule:MF_01911 |
Chain | Residue | Details |
A | ILE63-GLU86 | |
B | ILE63-GLU86 | |
C | ILE63-GLU86 | |
D | ILE63-GLU86 |