Research workbench
Crystal structure of fapr- a global regulator of fatty acid biosynthesis in B. subtilis
Analyse Crystal structure of fapr- a global regulator of fatty acid biosynthesis in B.… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 2F41
- Type
- protein
- Length
- 428 residues
- Chains
- 4
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Transcription factor fapr
- UniProt
- O34835
- Pockets
- 5 · best druggability 0.59
Structure
x-ray diffraction · 3 distinct chains · 16% helix, 53% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, D | Transcription factor fapr | protein | 108 | 16% helix, 51% strand | O34835 |
| B | Transcription factor fapr | protein | 109 | 16% helix, 54% strand | O34835 |
| C | Transcription factor fapr | protein | 103 | 17% helix, 53% strand | O34835 |
Pockets
5 pockets found on a 1 Å grid, 3 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 173 | 0.59 | 0.82 | 27 | empty |
| 2 | 166 | 0.55 | 0.80 | 25 | empty |
| 3 | 107 | 0.54 | 0.83 | 23 | empty |
| 4 | 141 | 0.47 | 0.77 | 22 | empty |
| 5 | 53 | 0.26 | 0.73 | 13 | empty |
Interfaces
2 interfaces between chains.
- A–B · 737 Ų buried · 9 hydrogen bonds · protein-protein
- C–D · 612 Ų buried · 6 hydrogen bonds · protein-protein
Compared structures
- 2F41 · Crystal structure of FapR- a global regulator of fatty acid biosynthesis in B. subtilis · the same entry in another collection · chain D against D, TM-score 1.00
- O34835 · AlphaFold monomer V2.0 prediction for transcription factor fapr (O34835) · a predicted model of the same protein · chain B against A, TM-score 0.99
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 O34835
- Elsewhere: RCSB PDB 2F41 · PDBe 2F41 · UniProt O34835
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