Research workbench
Flavin analogue sheds light on light-oxygen-voltage domain mechanism
Analyse Flavin analogue sheds light on light-oxygen-voltage domain mechanism in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 6I22
- Type
- protein
- Length
- 534 residues
- Chains
- 4
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- AUREOCHROME1-like protein
- UniProt
- C5NSW6
- Ligands
- FMN
- Pockets
- 7 · best druggability 0.70
Structure
x-ray diffraction · 2 distinct chains · 34% helix, 30% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, B | AUREOCHROME1-like protein | protein | 133 | 35% helix, 30% strand | C5NSW6 |
| C, D | AUREOCHROME1-like protein | protein | 134 | 34% helix, 29% strand | C5NSW6 |
Ligands and binding sites
- FMN · Flavin mononucleotide · ligand · 4 copies · chains A, B, C, D
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
7 pockets found on a 1 Å grid, 5 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 185 | 0.70 | 0.87 | 24 | FMN |
| 2 | 189 | 0.69 | 0.87 | 29 | FMN |
| 3 | 202 | 0.69 | 0.86 | 25 | FMN |
| 4 | 207 | 0.68 | 0.85 | 26 | FMN |
| 5 | 141 | 0.59 | 0.84 | 28 | empty |
Interfaces
3 interfaces between chains.
- A–B · 898 Ų buried · 9 hydrogen bonds · protein-protein
- C–D · 731 Ų buried · 4 hydrogen bonds · protein-protein
- A–C · 537 Ų buried · 6 hydrogen bonds · protein-protein
Compared structures
- 6I22 · Flavin Analogue Sheds Light on Light-Oxygen-Voltage Domain Mechanism · the same entry in another collection · chain B against B, 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 C5NSW6
- Elsewhere: RCSB PDB 6I22 · PDBe 6I22 · UniProt C5NSW6
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