6RXB
Crystal structure of TetR-Q116A from Acinetobacter baumannii AYE in complex with minocycline
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 | 0006355 | biological_process | regulation of DNA-templated transcription |
| A | 0045892 | biological_process | negative regulation of DNA-templated transcription |
| A | 0046677 | biological_process | response to antibiotic |
| B | 0003677 | molecular_function | DNA binding |
| B | 0003700 | molecular_function | DNA-binding transcription factor activity |
| B | 0006355 | biological_process | regulation of DNA-templated transcription |
| B | 0045892 | biological_process | negative regulation of DNA-templated transcription |
| B | 0046677 | biological_process | response to antibiotic |
| C | 0003677 | molecular_function | DNA binding |
| C | 0003700 | molecular_function | DNA-binding transcription factor activity |
| C | 0006355 | biological_process | regulation of DNA-templated transcription |
| C | 0045892 | biological_process | negative regulation of DNA-templated transcription |
| C | 0046677 | biological_process | response to antibiotic |
| D | 0003677 | molecular_function | DNA binding |
| D | 0003700 | molecular_function | DNA-binding transcription factor activity |
| D | 0006355 | biological_process | regulation of DNA-templated transcription |
| D | 0045892 | biological_process | negative regulation of DNA-templated transcription |
| D | 0046677 | biological_process | response to antibiotic |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 15 |
| Details | binding site for residue MIY B 301 |
| Chain | Residue |
| A | HOH402 |
| B | LEU134 |
| B | ARG135 |
| B | SER138 |
| B | MG302 |
| B | HOH407 |
| B | HOH433 |
| B | LEU60 |
| B | HIS64 |
| B | SER67 |
| B | ASN82 |
| B | PHE86 |
| B | HIS100 |
| B | ARG104 |
| B | PRO105 |
| site_id | AC2 |
| Number of Residues | 7 |
| Details | binding site for residue MG B 302 |
| Chain | Residue |
| A | GLU147 |
| A | HOH402 |
| B | HIS100 |
| B | THR103 |
| B | MIY301 |
| B | HOH402 |
| B | HOH433 |
| site_id | AC3 |
| Number of Residues | 15 |
| Details | binding site for residue MIY D 301 |
| Chain | Residue |
| C | HOH406 |
| D | LEU60 |
| D | HIS64 |
| D | SER67 |
| D | ASN82 |
| D | PHE86 |
| D | HIS100 |
| D | ARG104 |
| D | PRO105 |
| D | LEU134 |
| D | ARG135 |
| D | SER138 |
| D | MG302 |
| D | HOH401 |
| D | HOH414 |
| site_id | AC4 |
| Number of Residues | 7 |
| Details | binding site for residue MG D 302 |
| Chain | Residue |
| C | GLU147 |
| C | HOH406 |
| D | HIS100 |
| D | THR103 |
| D | MIY301 |
| D | HOH401 |
| D | HOH414 |
| site_id | AC5 |
| Number of Residues | 3 |
| Details | binding site for residue CL D 303 |
| Chain | Residue |
| D | ARG129 |
| D | HIS209 |
| D | HIS210 |
| site_id | AC6 |
| Number of Residues | 7 |
| Details | binding site for residue SIN D 304 |
| Chain | Residue |
| B | ALA61 |
| B | HIS64 |
| B | THR65 |
| B | SER67 |
| C | ASP182 |
| D | HIS210 |
| D | HIS211 |
| site_id | AC7 |
| Number of Residues | 17 |
| Details | binding site for residue MIY A 301 |
| Chain | Residue |
| A | HIS64 |
| A | SER67 |
| A | ASN82 |
| A | PHE86 |
| A | HIS100 |
| A | ARG104 |
| A | PRO105 |
| A | ALA113 |
| A | VAL131 |
| A | LEU134 |
| A | SER138 |
| A | MG302 |
| A | HOH403 |
| A | HOH423 |
| B | PHE176 |
| B | HOH401 |
| B | HOH406 |
| site_id | AC8 |
| Number of Residues | 5 |
| Details | binding site for residue MG A 302 |
| Chain | Residue |
| A | HIS100 |
| A | MIY301 |
| A | HOH423 |
| B | HOH401 |
| B | HOH406 |
| site_id | AC9 |
| Number of Residues | 3 |
| Details | binding site for residue EDO A 303 |
| Chain | Residue |
| A | ASP95 |
| A | ARG98 |
| A | HOH405 |
| site_id | AD1 |
| Number of Residues | 1 |
| Details | binding site for residue CL A 304 |
| Chain | Residue |
| A | ARG129 |
| site_id | AD2 |
| Number of Residues | 16 |
| Details | binding site for residue MIY C 301 |
| Chain | Residue |
| C | LEU60 |
| C | HIS64 |
| C | ASN82 |
| C | PHE86 |
| C | HIS100 |
| C | ARG104 |
| C | THR112 |
| C | VAL131 |
| C | LEU134 |
| C | ARG135 |
| C | SER138 |
| C | MG302 |
| C | HOH401 |
| C | HOH420 |
| D | PHE176 |
| D | HOH404 |
| site_id | AD3 |
| Number of Residues | 6 |
| Details | binding site for residue MG C 302 |
| Chain | Residue |
| C | HOH401 |
| C | HOH420 |
| D | HOH404 |
| C | HIS100 |
| C | THR103 |
| C | MIY301 |
Functional Information from PROSITE/UniProt
| site_id | PS01081 |
| Number of Residues | 32 |
| Details | HTH_TETR_1 TetR-type HTH domain signature. GMdslTTrkLaerlkVQqPaLYwHFqNKralL |
| Chain | Residue | Details |
| A | GLY21-LEU52 | |
| B | GLY21-LEU52 |
