Research workbench
Crystal structure of FDR9
Analyse Crystal structure of FDR9 in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 6TUK
- Type
- protein
- Length
- 393 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Putative oxidoreductase
- UniProt
- Q47QF8
- Ligands
- FAD, SO4
- Pockets
- 2 · best druggability 0.79
Structure
x-ray diffraction · 1 distinct chain · 25% helix, 30% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| B | Putative oxidoreductase | protein | 393 | 25% helix, 30% strand | Q47QF8 |
Ligands and binding sites
- FAD · Flavin-adenine dinucleotide · ligand · chains B
- SO4 · Sulfate ion · ion · 4 copies · chains B
- BU3 · (R,R)-2,3-butanediol · additive · 3 copies · chains B
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
2 pockets found on a 1 Å grid, 1 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 790 | 0.79 | 0.83 | 73 | FAD, BU3 |
| 2 | 57 | 0.28 | 0.74 | 13 | empty |
Compared structures
- 6TUK · Crystal structure of Fdr9 · 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 Q47QF8
- Elsewhere: RCSB PDB 6TUK · PDBe 6TUK · UniProt Q47QF8
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