Research workbench
SFX structure of D.m(6-4)photolyase
Analyse SFX structure of D.m(6-4)photolyase in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 8C1U
- Type
- protein
- Length
- 500 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v2 / PDB Bank
- Contract
- 0xd58B01f6C18086e5202cdC5D7Ad3E41790360102
- Owner
- 0xF4e1AA6f26B7DA48EeAD9B24a97927303eeA07b8
- Resolution
- 1.7
- Source
- Drosophila melanogaster
- Molecule
- Cryptochrome-1
- UniProt
- Q8SXK5
- Ligands
- FAD
- Pockets
- 5 · best druggability 0.82
Structure
x-ray diffraction · resolution 1.7 · 1 distinct chain · 49% helix, 7% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Cryptochrome-1 | protein | 500 | 49% helix, 7% strand | Q8SXK5 |
Ligands and binding sites
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
5 pockets found on a 1 Å grid, 2 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 469 | 0.82 | 0.89 | 44 | FAD, GOL |
| 2 | 245 | 0.80 | 0.92 | 39 | empty |
| 3 | 97 | 0.40 | 0.77 | 20 | empty |
| 4 | 86 | 0.37 | 0.76 | 19 | empty |
| 5 | 55 | 0.36 | 0.79 | 21 | empty |
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 Q8SXK5
- Elsewhere: RCSB PDB 8C1U · PDBe 8C1U · UniProt Q8SXK5
GL1X is a live explorer of the GenesisL1 blockchain. Turn on JavaScript for search, charts and interactive views.