6PFV
Structure of S. venezuelae RisG-WhiG-c-di-GMP complex: orthorhombic crystal form
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0003677 | molecular_function | DNA binding |
| A | 0003700 | molecular_function | DNA-binding transcription factor activity |
| A | 0003899 | molecular_function | DNA-directed RNA polymerase activity |
| A | 0006352 | biological_process | DNA-templated transcription initiation |
| A | 0006355 | biological_process | regulation of DNA-templated transcription |
| A | 0016987 | molecular_function | sigma factor activity |
| D | 0003677 | molecular_function | DNA binding |
| D | 0003700 | molecular_function | DNA-binding transcription factor activity |
| D | 0003899 | molecular_function | DNA-directed RNA polymerase activity |
| D | 0006352 | biological_process | DNA-templated transcription initiation |
| D | 0006355 | biological_process | regulation of DNA-templated transcription |
| D | 0016987 | molecular_function | sigma factor activity |
| G | 0003677 | molecular_function | DNA binding |
| G | 0003700 | molecular_function | DNA-binding transcription factor activity |
| G | 0003899 | molecular_function | DNA-directed RNA polymerase activity |
| G | 0006352 | biological_process | DNA-templated transcription initiation |
| G | 0006355 | biological_process | regulation of DNA-templated transcription |
| G | 0016987 | molecular_function | sigma factor activity |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 13 |
| Details | binding site for residue C2E T 201 |
| Chain | Residue |
| A | LYS57 |
| T | GLU162 |
| T | SER166 |
| T | ARG169 |
| T | C2E202 |
| T | ARG71 |
| T | GLN75 |
| T | ILE78 |
| T | ASP79 |
| T | ASP105 |
| T | SER108 |
| T | HIS110 |
| T | SER112 |
| site_id | AC2 |
| Number of Residues | 17 |
| Details | binding site for residue C2E T 202 |
| Chain | Residue |
| A | GLY61 |
| A | ARG62 |
| A | VAL65 |
| T | GLU64 |
| T | SER68 |
| T | ARG71 |
| T | ARG72 |
| T | ASP105 |
| T | VAL106 |
| T | PRO107 |
| T | SER108 |
| T | SER112 |
| T | ARG115 |
| T | ARG169 |
| T | GLN173 |
| T | ASP177 |
| T | C2E201 |
| site_id | AC3 |
| Number of Residues | 12 |
| Details | binding site for residue C2E B 201 |
| Chain | Residue |
| B | ARG71 |
| B | GLN75 |
| B | ILE78 |
| B | ASP79 |
| B | SER108 |
| B | HIS110 |
| B | SER112 |
| B | GLU162 |
| B | SER166 |
| B | ARG169 |
| B | C2E202 |
| D | LYS57 |
| site_id | AC4 |
| Number of Residues | 17 |
| Details | binding site for residue C2E B 202 |
| Chain | Residue |
| B | GLN61 |
| B | GLU64 |
| B | SER68 |
| B | ARG71 |
| B | ARG72 |
| B | ASP105 |
| B | VAL106 |
| B | SER108 |
| B | SER112 |
| B | ARG115 |
| B | ARG169 |
| B | GLN173 |
| B | ASP177 |
| B | C2E201 |
| D | GLY61 |
| D | ARG62 |
| D | VAL65 |
| site_id | AC5 |
| Number of Residues | 12 |
| Details | binding site for residue C2E E 201 |
| Chain | Residue |
| E | ARG71 |
| E | GLN75 |
| E | ILE78 |
| E | ASP79 |
| E | ARG82 |
| E | SER108 |
| E | HIS110 |
| E | GLU162 |
| E | SER166 |
| E | ARG169 |
| E | C2E202 |
| G | LYS57 |
| site_id | AC6 |
| Number of Residues | 16 |
| Details | binding site for residue C2E E 202 |
| Chain | Residue |
| E | GLU64 |
| E | SER68 |
| E | ARG71 |
| E | ARG72 |
| E | ASP105 |
| E | VAL106 |
| E | SER108 |
| E | SER112 |
| E | ARG115 |
| E | ARG169 |
| E | GLN173 |
| E | ALA176 |
| E | ASP177 |
| E | C2E201 |
| G | ARG62 |
| G | VAL65 |
Functional Information from PROSITE/UniProt
