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Structure of the regulator fasr from mycobacterium tuberculosis in complex with DNA
Analyse Structure of the regulator fasr from mycobacterium tuberculosis in complex with… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 6O6P
- Type
- protein + DNA
- Length
- 421 residues
- Chains
- 4
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Tetr family transcriptional regulator; DNA-forward; DNA-reverse
- UniProt
- O05858
- Pockets
- 7 · best druggability 0.81
Structure
x-ray diffraction · 4 distinct chains · 78% helix, 0% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Tetr family transcriptional regulator | protein | 188 | 78% helix, 0% strand | O05858 |
| B | Tetr family transcriptional regulator | protein | 187 | 78% helix, 0% strand | O05858 |
| C | DNA-forward | dna | 23 | — | — |
| D | DNA-reverse | dna | 23 | — | — |
Pockets
7 pockets found on a 1 Å grid, 4 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 792 | 0.81 | 0.84 | 73 | empty |
| 2 | 149 | 0.76 | 0.93 | 26 | empty |
| 3 | 97 | 0.71 | 0.93 | 23 | empty |
| 4 | 566 | 0.62 | 0.74 | 27 | empty |
| 5 | 57 | 0.47 | 0.85 | 15 | empty |
Interfaces
6 interfaces between chains.
- A–B · 1883 Ų buried · 10 hydrogen bonds · protein-protein
- C–D · 1122 Ų buried · 105 hydrogen bonds · nucleic-nucleic
- B–D · 322 Ų buried · 9 hydrogen bonds · protein-nucleic
- A–C · 298 Ų buried · 3 hydrogen bonds · protein-nucleic
- A–D · 199 Ų buried · 1 hydrogen bond · protein-nucleic
Compared structures
- 6O6P · Structure of the regulator FasR from Mycobacterium tuberculosis in complex with DNA · the same entry in another collection · chain A against A, TM-score 1.00
Analyse
- Open in the research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides and crosslinks on the 3D structure
- Every structure of UniProt O05858
- Elsewhere: RCSB PDB 6O6P · PDBe 6O6P · UniProt O05858
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