MolNFT v1 · #147525 · protein
The NADPH-dependent sulfite reductase flavoprotein adopts an extended conformation that is unique to this diflavin reductase
6EFV · Sulfite reductase [NADPH] flavoprotein alpha-component: “The NADPH-dependent sulfite reductase flavoprotein adopts an extended conformation that is unique to this…”. X-ray diffraction, 3 ligands (FAD, FMN, SO4), 4 pockets (best…
- PDB
- 6EFV
- Type
- protein
- Length
- 530 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Sulfite reductase [NADPH] flavoprotein alpha-component
- EC
- 1.8.1.2
- UniProt
- W8SX42
- Ligands
- FAD, FMN, SO4
- Pockets
- 4 · best druggability 0.58
Structure
x-ray diffraction · 1 distinct chain · 38% helix, 22% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Sulfite reductase [NADPH] flavoprotein alpha-component (EC 1.8.1.2) | protein | 530 | 38% helix, 22% strand | W8SX42 |
Ligands and binding sites
- FAD · Flavin-adenine dinucleotide · ligand · chains A
- FMN · Flavin mononucleotide · ligand · chains A
- SO4 · Sulfate ion · ion · 6 copies · chains A
- CXS · 3-cyclohexyl-1-propylsulfonic acid · additive · 2 copies · chains A
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
4 pockets found on a 1 Å grid, 1 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 384 | 0.58 | 0.75 | 48 | FAD |
| 2 | 55 | 0.41 | 0.82 | 21 | empty |
| 3 | 94 | 0.39 | 0.77 | 22 | FMN |
| 4 | 81 | 0.36 | 0.76 | 19 | CXS |
Compared structures
- 6EFV · The NADPH-dependent sulfite reductase flavoprotein adopts an extended conformation that… · the same entry in another collection · chain A against A, 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 W8SX42
- Elsewhere: RCSB PDB 6EFV · PDBe 6EFV · UniProt W8SX42
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