1NY6
Crystal structure of sigm54 activator (AAA+ ATPase) in the active state
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 |
| 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 |
| 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 |
| 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 |
| 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 |
| 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 |
| G | 0005524 | molecular_function | ATP binding |
| G | 0006355 | biological_process | regulation of DNA-templated transcription |
| G | 0008134 | molecular_function | transcription factor binding |
| G | 0016887 | molecular_function | ATP hydrolysis activity |
| H | 0005524 | molecular_function | ATP binding |
| H | 0006355 | biological_process | regulation of DNA-templated transcription |
| H | 0008134 | molecular_function | transcription factor binding |
| H | 0016887 | molecular_function | ATP hydrolysis activity |
| I | 0005524 | molecular_function | ATP binding |
| I | 0006355 | biological_process | regulation of DNA-templated transcription |
| I | 0008134 | molecular_function | transcription factor binding |
| I | 0016887 | molecular_function | ATP hydrolysis activity |
| J | 0005524 | molecular_function | ATP binding |
| J | 0006355 | biological_process | regulation of DNA-templated transcription |
| J | 0008134 | molecular_function | transcription factor binding |
| J | 0016887 | molecular_function | ATP hydrolysis activity |
| K | 0005524 | molecular_function | ATP binding |
| K | 0006355 | biological_process | regulation of DNA-templated transcription |
| K | 0008134 | molecular_function | transcription factor binding |
| K | 0016887 | molecular_function | ATP hydrolysis activity |
| L | 0005524 | molecular_function | ATP binding |
| L | 0006355 | biological_process | regulation of DNA-templated transcription |
| L | 0008134 | molecular_function | transcription factor binding |
| L | 0016887 | molecular_function | ATP hydrolysis activity |
| M | 0005524 | molecular_function | ATP binding |
| M | 0006355 | biological_process | regulation of DNA-templated transcription |
| M | 0008134 | molecular_function | transcription factor binding |
| M | 0016887 | molecular_function | ATP hydrolysis activity |
| N | 0005524 | molecular_function | ATP binding |
| N | 0006355 | biological_process | regulation of DNA-templated transcription |
| N | 0008134 | molecular_function | transcription factor binding |
| N | 0016887 | molecular_function | ATP hydrolysis activity |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 12 |
| Details | BINDING SITE FOR RESIDUE ADP C 1 |
| Chain | Residue |
| C | VAL140 |
| C | VAL356 |
| C | ARG357 |
| C | LYS360 |
| C | GLU168 |
| C | SER169 |
| C | GLY170 |
| C | VAL171 |
| C | GLY172 |
| C | LYS173 |
| C | GLU174 |
| C | VAL175 |
| site_id | AC2 |
| Number of Residues | 11 |
| Details | BINDING SITE FOR RESIDUE ADP D 2 |
| Chain | Residue |
| D | TYR139 |
| D | VAL140 |
| D | SER169 |
| D | GLY170 |
| D | VAL171 |
| D | GLY172 |
| D | LYS173 |
| D | GLU174 |
| D | VAL175 |
| D | VAL356 |
| D | ARG357 |
| site_id | AC3 |
| Number of Residues | 11 |
| Details | BINDING SITE FOR RESIDUE ADP E 3 |
| Chain | Residue |
| E | VAL140 |
| E | GLU168 |
| E | GLY170 |
| E | VAL171 |
| E | GLY172 |
| E | LYS173 |
| E | GLU174 |
| E | VAL175 |
| E | VAL356 |
| E | ARG357 |
| E | LYS360 |
| site_id | AC4 |
| Number of Residues | 11 |
| Details | BINDING SITE FOR RESIDUE ADP F 4 |
| Chain | Residue |
| F | VAL140 |
| F | GLY170 |
| F | VAL171 |
| F | GLY172 |
| F | LYS173 |
| F | GLU174 |
| F | VAL175 |
| F | LEU320 |
| F | VAL356 |
| F | ARG357 |
| F | LYS360 |
| site_id | AC5 |
| Number of Residues | 10 |
| Details | BINDING SITE FOR RESIDUE ADP G 5 |
| Chain | Residue |
| G | VAL140 |
| G | SER169 |
| G | GLY170 |
| G | VAL171 |
| G | GLY172 |
| G | LYS173 |
| G | GLU174 |
| G | VAL175 |
| G | VAL356 |
| G | ARG357 |
| site_id | AC6 |
| Number of Residues | 12 |
| Details | BINDING SITE FOR RESIDUE ADP A 6 |
| Chain | Residue |
| A | VAL140 |
| A | SER169 |
| A | GLY170 |
| A | VAL171 |
| A | GLY172 |
| A | LYS173 |
| A | GLU174 |
| A | VAL175 |
| A | LEU320 |
| A | VAL356 |
| A | ARG357 |
| A | LYS360 |
| site_id | AC7 |
| Number of Residues | 10 |
| Details | BINDING SITE FOR RESIDUE ADP B 7 |
| Chain | Residue |
| B | GLY170 |
| B | VAL171 |
| B | GLY172 |
| B | LYS173 |
| B | GLU174 |
| B | VAL175 |
| B | LEU320 |
| B | VAL356 |
| B | ARG357 |
| B | LYS360 |
| site_id | AC8 |
| Number of Residues | 14 |
| Details | BINDING SITE FOR RESIDUE ADP I 8 |
| Chain | Residue |
| I | TYR139 |
| I | VAL140 |
| I | PHE141 |
| I | MET146 |
| I | GLU168 |
| I | GLY170 |
| I | VAL171 |
| I | GLY172 |
| I | LYS173 |
| I | GLU174 |
| I | VAL175 |
| I | VAL356 |
| I | ARG357 |
| I | LYS360 |
| site_id | AC9 |
| Number of Residues | 10 |
| Details | BINDING SITE FOR RESIDUE ADP J 9 |
| Chain | Residue |
| J | ARG357 |
| J | LYS360 |
| J | VAL140 |
| J | GLY170 |
| J | VAL171 |
| J | GLY172 |
| J | LYS173 |
| J | GLU174 |
| J | VAL175 |
| J | VAL356 |
| site_id | BC1 |
| Number of Residues | 11 |
| Details | BINDING SITE FOR RESIDUE ADP K 10 |
| Chain | Residue |
| K | VAL140 |
| K | SER169 |
| K | GLY170 |
| K | VAL171 |
| K | GLY172 |
| K | LYS173 |
| K | GLU174 |
| K | VAL175 |
| K | VAL356 |
| K | ARG357 |
| K | LYS360 |
| site_id | BC2 |
| Number of Residues | 11 |
| Details | BINDING SITE FOR RESIDUE ADP L 11 |
| Chain | Residue |
| L | VAL140 |
| L | PHE141 |
| L | GLY170 |
| L | VAL171 |
| L | GLY172 |
| L | LYS173 |
| L | GLU174 |
| L | VAL175 |
| L | VAL356 |
| L | ARG357 |
| L | LYS360 |
| site_id | BC3 |
| Number of Residues | 12 |
| Details | BINDING SITE FOR RESIDUE ADP M 12 |
| Chain | Residue |
| M | TYR139 |
| M | VAL140 |
| M | PHE141 |
| M | GLY170 |
| M | VAL171 |
| M | GLY172 |
| M | LYS173 |
| M | GLU174 |
| M | VAL175 |
| M | VAL356 |
| M | ARG357 |
| M | LYS360 |
| site_id | BC4 |
| Number of Residues | 9 |
| Details | BINDING SITE FOR RESIDUE ADP N 13 |
| Chain | Residue |
| N | VAL140 |
| N | GLU168 |
| N | GLY170 |
| N | VAL171 |
| N | GLY172 |
| N | LYS173 |
| N | GLU174 |
| N | VAL175 |
| N | VAL356 |
| site_id | BC5 |
| Number of Residues | 12 |
| Details | BINDING SITE FOR RESIDUE ADP H 14 |
| Chain | Residue |
| H | PHE141 |
| H | GLU168 |
| H | GLY170 |
| H | VAL171 |
| H | GLY172 |
| H | LYS173 |
| H | GLU174 |
| H | VAL175 |
| H | VAL356 |
| H | ARG357 |
| H | LYS360 |
| N | GLU256 |
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. VLItGESGVGKevV |
| Chain | Residue | Details |
| A | VAL163-VAL176 |
| site_id | PS00676 |
| Number of Residues | 16 |
| Details | SIGMA54_INTERACT_2 Sigma-54 interaction domain ATP-binding region B signature. GfFelADGGTLFLDEI |
| Chain | Residue | Details |
| A | GLY225-ILE240 |
