5M7N
Crystal structure of NtrX from Brucella abortus in complex with ATP processed with the CrystalDirect automated mounting and cryo-cooling technology
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0000160 | biological_process | phosphorelay signal transduction system |
| 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 | 0000160 | biological_process | phosphorelay signal transduction system |
| 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 |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 4 |
| Details | binding site for residue MG A 501 |
| Chain | Residue |
| A | ASP9 |
| A | ASP10 |
| A | ASP53 |
| A | HOH643 |
| site_id | AC2 |
| Number of Residues | 14 |
| Details | binding site for residue ATP A 502 |
| Chain | Residue |
| A | GLY175 |
| A | LYS176 |
| A | GLU177 |
| A | LEU178 |
| A | LEU319 |
| A | LEU355 |
| A | ARG356 |
| B | ALA331 |
| B | ARG370 |
| A | LEU142 |
| A | VAL143 |
| A | MET149 |
| A | GLY173 |
| A | ALA174 |
| site_id | AC3 |
| Number of Residues | 4 |
| Details | binding site for residue MG B 501 |
| Chain | Residue |
| B | ASP9 |
| B | ASP10 |
| B | ASP53 |
| B | LYS105 |
| site_id | AC4 |
| Number of Residues | 15 |
| Details | binding site for residue ATP B 502 |
| Chain | Residue |
| A | ALA331 |
| A | ARG370 |
| B | LEU142 |
| B | VAL143 |
| B | MET149 |
| B | GLY173 |
| B | ALA174 |
| B | GLY175 |
| B | LYS176 |
| B | GLU177 |
| B | LEU178 |
| B | LEU355 |
| B | ARG356 |
| B | ARG359 |
| B | HOH615 |
Functional Information from PROSITE/UniProt
| site_id | PS00676 |
| Number of Residues | 16 |
| Details | SIGMA54_INTERACT_2 Sigma-54 interaction domain ATP-binding region B signature. GaLeeAHGGILYLDEV |
| Chain | Residue | Details |
| A | GLY224-VAL239 |
| site_id | PS00688 |
| Number of Residues | 10 |
| Details | SIGMA54_INTERACT_3 Sigma-54 interaction domain C-terminal part signature. WPGNLRQLrN |
| Chain | Residue | Details |
| A | TRP351-ASN360 |
