1OJL
Crystal structure of a sigma54-activator suggests the mechanism for the conformational switch necessary for sigma54 binding
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0005524 | molecular_function | ATP binding |
| A | 0006355 | biological_process | regulation of DNA-templated transcription |
| A | 0008134 | molecular_function | transcription factor binding |
| A | 0016887 | molecular_function | ATP hydrolysis activity |
| A | 0043565 | molecular_function | sequence-specific DNA binding |
| B | 0005524 | molecular_function | ATP binding |
| B | 0006355 | biological_process | regulation of DNA-templated transcription |
| B | 0008134 | molecular_function | transcription factor binding |
| B | 0016887 | molecular_function | ATP hydrolysis activity |
| B | 0043565 | molecular_function | sequence-specific DNA binding |
| C | 0005524 | molecular_function | ATP binding |
| C | 0006355 | biological_process | regulation of DNA-templated transcription |
| C | 0008134 | molecular_function | transcription factor binding |
| C | 0016887 | molecular_function | ATP hydrolysis activity |
| C | 0043565 | molecular_function | sequence-specific DNA binding |
| D | 0005524 | molecular_function | ATP binding |
| D | 0006355 | biological_process | regulation of DNA-templated transcription |
| D | 0008134 | molecular_function | transcription factor binding |
| D | 0016887 | molecular_function | ATP hydrolysis activity |
| D | 0043565 | molecular_function | sequence-specific DNA binding |
| E | 0005524 | molecular_function | ATP binding |
| E | 0006355 | biological_process | regulation of DNA-templated transcription |
| E | 0008134 | molecular_function | transcription factor binding |
| E | 0016887 | molecular_function | ATP hydrolysis activity |
| E | 0043565 | molecular_function | sequence-specific DNA binding |
| F | 0005524 | molecular_function | ATP binding |
| F | 0006355 | biological_process | regulation of DNA-templated transcription |
| F | 0008134 | molecular_function | transcription factor binding |
| F | 0016887 | molecular_function | ATP hydrolysis activity |
| F | 0043565 | molecular_function | sequence-specific DNA binding |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE PO4 A1442 |
| Chain | Residue |
| A | SER171 |
| A | GLY172 |
| A | THR173 |
| A | LYS175 |
| A | ARG359 |
| site_id | AC2 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE PO4 B1390 |
| Chain | Residue |
| B | ARG359 |
| B | SER171 |
| B | GLY172 |
| B | THR173 |
| B | LYS175 |
| site_id | AC3 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE PO4 C1391 |
| Chain | Residue |
| C | ASP170 |
| C | SER171 |
| C | GLY172 |
| C | THR173 |
| C | LYS175 |
| C | ARG359 |
| site_id | AC4 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE PO4 D1442 |
| Chain | Residue |
| D | SER171 |
| D | GLY172 |
| D | THR173 |
| D | LYS175 |
| D | ARG359 |
| site_id | AC5 |
| Number of Residues | 7 |
| Details | BINDING SITE FOR RESIDUE PO4 F1390 |
| Chain | Residue |
| F | SER171 |
| F | GLY172 |
| F | THR173 |
| F | LYS175 |
| F | GLU176 |
| F | ASP240 |
| F | ARG359 |
| site_id | AC6 |
| Number of Residues | 15 |
| Details | BINDING SITE FOR RESIDUE ATP E1442 |
| Chain | Residue |
| E | ILE142 |
| E | SER171 |
| E | GLY172 |
| E | THR173 |
| E | GLY174 |
| E | LYS175 |
| E | GLU176 |
| E | ASP240 |
| E | ARG315 |
| E | LEU322 |
| E | PHE326 |
| E | ARG329 |
| E | ILE358 |
| E | ARG359 |
| E | GLU362 |
Functional Information from PROSITE/UniProt
| site_id | PS00675 |
| Number of Residues | 14 |
| Details | SIGMA54_INTERACT_1 Sigma-54 interaction domain ATP-binding region A signature. VLIhGDSGTGKelV |
| Chain | Residue | Details |
| A | VAL165-VAL178 |
| site_id | PS00676 |
| Number of Residues | 16 |
| Details | SIGMA54_INTERACT_2 Sigma-54 interaction domain ATP-binding region B signature. GrFveADGGTLFLDEI |
| Chain | Residue | Details |
| A | GLY227-ILE242 |
| site_id | PS00688 |
| Number of Residues | 10 |
| Details | SIGMA54_INTERACT_3 Sigma-54 interaction domain C-terminal part signature. WPGNIRELeN |
| Chain | Residue | Details |
| A | TRP354-ASN363 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 114 |
| Details | DNA_BIND: H-T-H motif => ECO:0000250 |
| Chain | Residue | Details |
| A | LYS421-SER440 | |
| B | LYS421-SER440 | |
| C | LYS421-SER440 | |
| D | LYS421-SER440 | |
| E | LYS421-SER440 | |
| F | LYS421-SER440 |
| site_id | SWS_FT_FI2 |
| Number of Residues | 24 |
| Details | BINDING: BINDING => ECO:0000269|PubMed:16005641, ECO:0007744|PDB:1OJL |
| Chain | Residue | Details |
| A | GLY172 | |
| C | THR173 | |
| C | ARG329 | |
| C | ARG359 | |
| D | GLY172 | |
| D | THR173 | |
| D | ARG329 | |
| D | ARG359 | |
| E | GLY172 | |
| E | THR173 | |
| E | ARG329 | |
| A | THR173 | |
| E | ARG359 | |
| F | GLY172 | |
| F | THR173 | |
| F | ARG329 | |
| F | ARG359 | |
| A | ARG329 | |
| A | ARG359 | |
| B | GLY172 | |
| B | THR173 | |
| B | ARG329 | |
| B | ARG359 | |
| C | GLY172 |
Catalytic Information from CSA
| site_id | CSA1 |
| Number of Residues | 1 |
| Details | Annotated By Reference To The Literature 1g8p |
| Chain | Residue | Details |
| A | ARG380 |
| site_id | CSA2 |
| Number of Residues | 1 |
| Details | Annotated By Reference To The Literature 1g8p |
| Chain | Residue | Details |
| B | ARG380 |
| site_id | CSA3 |
| Number of Residues | 1 |
| Details | Annotated By Reference To The Literature 1g8p |
| Chain | Residue | Details |
| C | ARG380 |
| site_id | CSA4 |
| Number of Residues | 1 |
| Details | Annotated By Reference To The Literature 1g8p |
| Chain | Residue | Details |
| D | ARG380 |
| site_id | CSA5 |
| Number of Residues | 1 |
| Details | Annotated By Reference To The Literature 1g8p |
| Chain | Residue | Details |
| E | ARG380 |
| site_id | CSA6 |
| Number of Residues | 1 |
| Details | Annotated By Reference To The Literature 1g8p |
| Chain | Residue | Details |
| F | ARG380 |
