Research workbench
Crystal structure of ssue FMN reductase Y118A mutant in FMN bound form.
Analyse Crystal structure of ssue FMN reductase Y118A mutant in FMN bound form. in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 6DQO
- Type
- protein
- Length
- 173 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- FMN reductase (NADPH)
- EC
- 1.5.1.38
- UniProt
- P80644
- Ligands
- FMN
- Pockets
- 1 · best druggability 0.31
Structure
x-ray diffraction · 1 distinct chain · 46% helix, 23% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | FMN reductase (NADPH) (EC 1.5.1.38) | protein | 173 | 46% helix, 23% strand | P80644 |
Ligands and binding sites
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
1 pocket found on a 1 Å grid, 0 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 56 | 0.31 | 0.76 | 18 | empty |
Compared structures
- 6DQO · Crystal structure of SsuE FMN reductase Y118A mutant in FMN bound form. · the same entry in another collection · chain A against A, TM-score 1.00
- P80644 · AlphaFold monomer V2.0 prediction for FMN reductase (NADPH) (P80644) · a predicted model of the same protein · chain A against A, TM-score 0.98
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 P80644
- Elsewhere: RCSB PDB 6DQO · PDBe 6DQO · UniProt P80644
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