5X80
CRYSTAL STRUCTURE OF MYCOBACTERIUM TUBERCULOSIS MARR FAMILY PROTEIN RV2887 COMPLEX WITH SALICYLIC ACID
Replaces: 5HSNFunctional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0003677 | molecular_function | DNA binding |
| A | 0003700 | molecular_function | DNA-binding transcription factor activity |
| A | 0006351 | biological_process | DNA-templated transcription |
| A | 0006355 | biological_process | regulation of DNA-templated transcription |
| A | 0006950 | biological_process | response to stress |
| B | 0003677 | molecular_function | DNA binding |
| B | 0003700 | molecular_function | DNA-binding transcription factor activity |
| B | 0006351 | biological_process | DNA-templated transcription |
| B | 0006355 | biological_process | regulation of DNA-templated transcription |
| B | 0006950 | biological_process | response to stress |
| C | 0003677 | molecular_function | DNA binding |
| C | 0003700 | molecular_function | DNA-binding transcription factor activity |
| C | 0006351 | biological_process | DNA-templated transcription |
| C | 0006355 | biological_process | regulation of DNA-templated transcription |
| C | 0006950 | biological_process | response to stress |
| D | 0003677 | molecular_function | DNA binding |
| D | 0003700 | molecular_function | DNA-binding transcription factor activity |
| D | 0006351 | biological_process | DNA-templated transcription |
| D | 0006355 | biological_process | regulation of DNA-templated transcription |
| D | 0006950 | biological_process | response to stress |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 4 |
| Details | binding site for residue SAL A 201 |
| Chain | Residue |
| A | PHE38 |
| A | ARG42 |
| B | PRO8 |
| B | GLY10 |
| site_id | AC2 |
| Number of Residues | 5 |
| Details | binding site for residue SO4 B 201 |
| Chain | Residue |
| A | TYR14 |
| B | GLU54 |
| B | ARG57 |
| B | HIS58 |
| B | HOH308 |
| site_id | AC3 |
| Number of Residues | 4 |
| Details | binding site for residue SO4 B 202 |
| Chain | Residue |
| B | SER51 |
| B | ALA53 |
| B | GLU54 |
| B | ARG57 |
| site_id | AC4 |
| Number of Residues | 4 |
| Details | binding site for residue SAL B 203 |
| Chain | Residue |
| A | PRO8 |
| B | PHE38 |
| B | ARG42 |
| B | HOH307 |
| site_id | AC5 |
| Number of Residues | 5 |
| Details | binding site for residue SAL C 201 |
| Chain | Residue |
| C | PHE38 |
| C | ARG42 |
| C | HOH302 |
| D | PRO8 |
| D | GLY10 |
| site_id | AC6 |
| Number of Residues | 3 |
| Details | binding site for residue SAL D 201 |
| Chain | Residue |
| C | TYR11 |
| D | PHE38 |
| D | ARG42 |
Functional Information from PROSITE/UniProt
| site_id | PS01117 |
| Number of Residues | 36 |
| Details | HTH_MARR_1 MarR-type HTH domain signature. QAmNtvlrkLEdaGAVarpasvsSGRslpatlTarG |
| Chain | Residue | Details |
| A | GLN64-GLY99 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 8 |
| Details | Binding site: {"evidences":[{"source":"PubMed","id":"28743871","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
