4YZE
Crystal structure of E.coli NemR reduced 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 | 0005515 | molecular_function | protein binding |
| A | 0045892 | biological_process | negative regulation of DNA-templated transcription |
| B | 0003677 | molecular_function | DNA binding |
| B | 0003700 | molecular_function | DNA-binding transcription factor activity |
| B | 0005515 | molecular_function | protein binding |
| B | 0045892 | biological_process | negative regulation of DNA-templated transcription |
| C | 0003677 | molecular_function | DNA binding |
| C | 0003700 | molecular_function | DNA-binding transcription factor activity |
| C | 0005515 | molecular_function | protein binding |
| C | 0045892 | biological_process | negative regulation of DNA-templated transcription |
| D | 0003677 | molecular_function | DNA binding |
| D | 0003700 | molecular_function | DNA-binding transcription factor activity |
| D | 0005515 | molecular_function | protein binding |
| D | 0045892 | biological_process | negative regulation of DNA-templated transcription |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 120 |
| Details | Domain: {"description":"HTH tetR-type","evidences":[{"source":"PROSITE-ProRule","id":"PRU00335","evidenceCode":"ECO:0000255"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI2 |
| Number of Residues | 76 |
| Details | DNA binding: {"description":"H-T-H motif","evidences":[{"source":"PROSITE-ProRule","id":"PRU00335","evidenceCode":"ECO:0000255"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI3 |
| Number of Residues | 4 |
| Details | Site: {"description":"Plays a central role in response to RCS","evidences":[{"source":"PubMed","id":"23536188","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"25867078","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |






