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Crystal structure of ssue FMN reductase Y118A mutant in apo form.
Analyse Crystal structure of ssue FMN reductase Y118A mutant in apo form. in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 6DQI
- Type
- protein
- Length
- 348 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- FMN reductase (NADPH)
- EC
- 1.5.1.38
- UniProt
- P80644
- Ligands
- SO4
- Pockets
- 2 · best druggability 0.41
Structure
x-ray diffraction · 2 distinct chains · 47% helix, 23% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | FMN reductase (NADPH) (EC 1.5.1.38) | protein | 175 | 47% helix, 23% strand | P80644 |
| B | FMN reductase (NADPH) (EC 1.5.1.38) | protein | 173 | 46% helix, 23% strand | P80644 |
Ligands and binding sites
- SO4 · Sulfate ion · ion · chains A
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
2 pockets found on a 1 Å grid, 0 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 113 | 0.41 | 0.76 | 25 | SO4 |
| 2 | 63 | 0.33 | 0.76 | 22 | empty |
Interfaces
1 interface between chains.
- A–B · 1160 Ų buried · 13 hydrogen bonds · protein-protein
Compared structures
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 6DQI · PDBe 6DQI · UniProt P80644
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