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Structure of Chloroflexus aggregans flavin based fluorescent protein (CagFbFP) Q148H variant
Analyse Structure of Chloroflexus aggregans flavin based fluorescent protein (CagFbFP)… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 6YWQ
- Type
- protein
- Length
- 211 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v2 / PDB Bank
- Contract
- 0xd58B01f6C18086e5202cdC5D7Ad3E41790360102
- Owner
- 0xF4e1AA6f26B7DA48EeAD9B24a97927303eeA07b8
- Resolution
- 1.27
- Source
- Chloroflexus aggregans (strain MD-66 / DSM 9485)
- Molecule
- Multi-sensor hybrid histidine kinase
- UniProt
- B8GAY9
- Ligands
- FMN
- Pockets
- 3 · best druggability 0.74
Structure
x-ray diffraction · resolution 1.27 · 2 distinct chains · 26% helix, 38% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Multi-sensor hybrid histidine kinase | protein | 106 | 25% helix, 38% strand | B8GAY9 |
| B | Multi-sensor hybrid histidine kinase | protein | 105 | 27% helix, 38% strand | B8GAY9 |
Ligands and binding sites
- FMN · Flavin mononucleotide · ligand · 2 copies · chains A, B
- GOL · Glycerol · additive · 2 copies · chains B
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
3 pockets found on a 1 Å grid, 2 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 164 | 0.74 | 0.91 | 22 | FMN |
| 2 | 164 | 0.72 | 0.90 | 23 | FMN |
| 3 | 130 | 0.42 | 0.76 | 20 | empty |
Interfaces
1 interface between chains.
- A–B · 608 Ų buried · 2 hydrogen bonds · protein-protein
Compared structures
- 6YWQ · Structure of chloroflexus aggregans flavin based fluorescent protein (cagfbfp) Q148H… · 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 B8GAY9
- Elsewhere: RCSB PDB 6YWQ · PDBe 6YWQ · UniProt B8GAY9
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