5M7O
Crystal structure of NtrX from Brucella abortus 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 | 7 |
Details | binding site for residue MG A 501 |
Chain | Residue |
A | ASP9 |
A | ASP10 |
A | GLU11 |
A | ASP53 |
A | LYS105 |
A | HOH618 |
A | HOH658 |
site_id | AC2 |
Number of Residues | 7 |
Details | binding site for residue MG B 501 |
Chain | Residue |
B | GLU11 |
B | ASP53 |
B | LYS105 |
B | HOH606 |
B | HOH637 |
B | ASP9 |
B | ASP10 |
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 |