Research workbench
Crystal Structure of Ferredoxin-NADP Reductase from Salmonella typhimurium
Analyse Crystal Structure of Ferredoxin-NADP Reductase from Salmonella typhimurium in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 3FPK
- Type
- protein
- Length
- 494 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v2 / PDB Bank
- Contract
- 0xd58B01f6C18086e5202cdC5D7Ad3E41790360102
- Owner
- 0xF4e1AA6f26B7DA48EeAD9B24a97927303eeA07b8
- Resolution
- 1.7
- Source
- Salmonella typhimurium
- Molecule
- Ferredoxin-NADP reductase
- EC
- 1.18.1.2
- UniProt
- Q8ZKP5
- Ligands
- FAD, MG, CA
- Pockets
- 7 · best druggability 0.66
Structure
x-ray diffraction · resolution 1.7 · 1 distinct chain · 25% helix, 34% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, B | Ferredoxin-NADP reductase (EC 1.18.1.2) | protein | 247 | 25% helix, 34% strand | Q8ZKP5 |
Ligands and binding sites
- FAD · Flavin-adenine dinucleotide · ligand · 2 copies · chains A, B
- MG · Magnesium ion · metal · 2 copies · chains A, B
- CA · Calcium ion · metal · chains B
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
7 pockets found on a 1 Å grid, 3 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 99 | 0.66 | 0.90 | 28 | empty |
| 2 | 324 | 0.63 | 0.79 | 44 | FAD |
| 3 | 335 | 0.60 | 0.77 | 42 | FAD |
| 4 | 117 | 0.40 | 0.76 | 23 | empty |
| 5 | 72 | 0.38 | 0.78 | 16 | MG |
Interfaces
1 interface between chains.
- A–B · 1045 Ų buried · 9 hydrogen bonds · protein-protein
Compared structures
- 3FPK · Crystal structure of ferredoxin-NADP reductase from salmonella typhimurium · 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 Q8ZKP5
- Elsewhere: RCSB PDB 3FPK · PDBe 3FPK · UniProt Q8ZKP5
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