Research workbench
Ferredoxin-NADP reductase
Analyse Ferredoxin-NADP reductase in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 2B5O
- Type
- protein
- Length
- 584 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Ferredoxin--NADP reductase
- EC
- 1.18.1.2
- UniProt
- P31973
- Ligands
- FAD, SO4
- Pockets
- 4 · best druggability 0.51
Structure
x-ray diffraction · 1 distinct chain · 27% helix, 30% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, B | Ferredoxin--NADP reductase (EC 1.18.1.2) | protein | 292 | 27% helix, 30% strand | P31973 |
Ligands and binding sites
- FAD · Flavin-adenine dinucleotide · ligand · 2 copies · chains A, B
- SO4 · Sulfate ion · ion · 11 copies · chains A, B
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 | 147 | 0.51 | 0.79 | 20 | FAD |
| 2 | 163 | 0.48 | 0.77 | 27 | FAD |
| 3 | 50 | 0.33 | 0.78 | 9 | empty |
| 4 | 66 | 0.31 | 0.75 | 17 | empty |
Interfaces
1 interface between chains.
- A–B · 1123 Ų buried · 29 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 P31973
- Elsewhere: RCSB PDB 2B5O · PDBe 2B5O · UniProt P31973
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