5XT2
Crystal structures of full-length FixJ from B. japonicum crystallized in space group P212121
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0000160 | biological_process | phosphorelay signal transduction system |
| A | 0003677 | molecular_function | DNA binding |
| A | 0006355 | biological_process | regulation of DNA-templated transcription |
| B | 0000160 | biological_process | phosphorelay signal transduction system |
| B | 0003677 | molecular_function | DNA binding |
| B | 0006355 | biological_process | regulation of DNA-templated transcription |
| C | 0000160 | biological_process | phosphorelay signal transduction system |
| C | 0003677 | molecular_function | DNA binding |
| C | 0006355 | biological_process | regulation of DNA-templated transcription |
| D | 0000160 | biological_process | phosphorelay signal transduction system |
| D | 0003677 | molecular_function | DNA binding |
| D | 0006355 | biological_process | regulation of DNA-templated transcription |
| E | 0000160 | biological_process | phosphorelay signal transduction system |
| E | 0003677 | molecular_function | DNA binding |
| E | 0006355 | biological_process | regulation of DNA-templated transcription |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 6 |
| Details | binding site for residue MG A 301 |
| Chain | Residue |
| A | ASP12 |
| A | ASP55 |
| A | HOH403 |
| A | HOH407 |
| A | HOH409 |
| B | ASP13 |
| site_id | AC2 |
| Number of Residues | 4 |
| Details | binding site for residue GOL A 302 |
| Chain | Residue |
| A | PHE107 |
| A | SER19 |
| A | LEU23 |
| A | PRO106 |
| site_id | AC3 |
| Number of Residues | 5 |
| Details | binding site for residue GOL A 303 |
| Chain | Residue |
| A | VAL140 |
| A | ALA141 |
| A | LEU143 |
| A | PRO145 |
| A | ARG148 |
| site_id | AC4 |
| Number of Residues | 3 |
| Details | binding site for residue GOL A 304 |
| Chain | Residue |
| A | ARG17 |
| A | LEU33 |
| A | ASP35 |
| site_id | AC5 |
| Number of Residues | 4 |
| Details | binding site for residue FMT A 305 |
| Chain | Residue |
| A | GLY84 |
| A | ASP87 |
| A | LYS105 |
| B | ASP13 |
| site_id | AC6 |
| Number of Residues | 3 |
| Details | binding site for residue FMT A 307 |
| Chain | Residue |
| A | LEU158 |
| A | SER159 |
| A | LEU190 |
| site_id | AC7 |
| Number of Residues | 6 |
| Details | binding site for residue MG B 301 |
| Chain | Residue |
| A | ASP13 |
| A | HOH412 |
| B | ASP12 |
| B | ASP55 |
| B | HOH407 |
| B | HOH410 |
| site_id | AC8 |
| Number of Residues | 6 |
| Details | binding site for residue FMT B 302 |
| Chain | Residue |
| A | ASP13 |
| A | ALA15 |
| A | HOH412 |
| B | GLY84 |
| B | ASP87 |
| B | LYS105 |
| site_id | AC9 |
| Number of Residues | 5 |
| Details | binding site for residue MG C 301 |
| Chain | Residue |
| C | ASP12 |
| C | ASP55 |
| C | HOH404 |
| C | HOH417 |
| C | HOH421 |
| site_id | AD1 |
| Number of Residues | 4 |
| Details | binding site for residue GOL C 302 |
| Chain | Residue |
| C | SER26 |
| C | GLY28 |
| D | LEU143 |
| D | SER144 |
| site_id | AD2 |
| Number of Residues | 4 |
| Details | binding site for residue GOL C 303 |
| Chain | Residue |
| C | ALA141 |
| C | SER142 |
| C | LEU143 |
| C | SER144 |
| site_id | AD3 |
| Number of Residues | 2 |
| Details | binding site for residue GOL C 304 |
| Chain | Residue |
| C | LEU33 |
| C | ASP35 |
| site_id | AD4 |
| Number of Residues | 3 |
| Details | binding site for residue GOL C 305 |
| Chain | Residue |
| C | MET16 |
| C | SER19 |
| C | PHE107 |
| site_id | AD5 |
| Number of Residues | 3 |
| Details | binding site for residue FMT C 306 |
| Chain | Residue |
| A | HIS85 |
| C | ARG178 |
| C | HOH408 |
| site_id | AD6 |
| Number of Residues | 6 |
| Details | binding site for residue MG D 301 |
| Chain | Residue |
| D | ASP11 |
| D | ASP12 |
| D | ASP55 |
| D | HOH401 |
| D | HOH418 |
| D | HOH419 |
| site_id | AD7 |
| Number of Residues | 5 |
| Details | binding site for residue GOL D 302 |
| Chain | Residue |
| D | MET16 |
| D | SER19 |
| D | LEU20 |
| D | PRO106 |
| D | PHE107 |
| site_id | AD8 |
| Number of Residues | 3 |
| Details | binding site for residue FMT D 303 |
| Chain | Residue |
| C | GLY30 |
| C | VAL31 |
| C | HOH403 |
| site_id | AD9 |
| Number of Residues | 2 |
| Details | binding site for residue FMT D 304 |
| Chain | Residue |
| D | ARG178 |
| D | HOH404 |
| site_id | AE1 |
| Number of Residues | 2 |
| Details | binding site for residue MG E 301 |
| Chain | Residue |
| E | ASP12 |
| E | ASP55 |
Functional Information from PROSITE/UniProt
| site_id | PS00622 |
| Number of Residues | 28 |
| Details | HTH_LUXR_1 LuxR-type HTH domain signature. GlsNklIAreYdIsprTIevYraNVmtK |
| Chain | Residue | Details |
| A | GLY157-LYS184 |
