Research workbench
Structure of chloroflexus aggregans flavin based fluorescent protein (cagfbfp) Q148D 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
- 6YWH
- Type
- protein
- Length
- 212 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Multi-sensor hybrid histidine kinase
- UniProt
- B8GAY9
- Ligands
- FMN
- Pockets
- 3 · best druggability 0.72
Structure
x-ray diffraction · 2 distinct chains · 25% helix, 36% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Multi-sensor hybrid histidine kinase | protein | 108 | 25% helix, 36% strand | B8GAY9 |
| B | Multi-sensor hybrid histidine kinase | protein | 104 | 26% helix, 37% strand | B8GAY9 |
Ligands and binding sites
- FMN · Flavin mononucleotide · ligand · 2 copies · chains A, B
- MES · 2-(N-morpholino)-ethanesulfonic acid · additive · chains A
- PG4 · Tetraethylene glycol · additive · chains A
- PGE · Triethylene glycol · additive · chains A
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 | 162 | 0.72 | 0.90 | 24 | FMN |
| 2 | 165 | 0.72 | 0.90 | 23 | FMN |
| 3 | 127 | 0.42 | 0.76 | 22 | empty |
Interfaces
1 interface between chains.
- A–B · 753 Ų buried · 6 hydrogen bonds · protein-protein
Compared structures
- 6YWH · Structure of Chloroflexus aggregans flavin based fluorescent protein (CagFbFP) Q148D… · 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 6YWH · PDBe 6YWH · UniProt B8GAY9
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