Research workbench
Crystal structure of ferredoxin-NADP reductase from burkholderia thailandensis E264 with bound FAD
Analyse Crystal structure of ferredoxin-NADP reductase from burkholderia thailandensis… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 4FK8
- Type
- protein
- Length
- 493 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
- Q2T230
- Ligands
- FAD
- Pockets
- 5 · best druggability 0.64
Structure
x-ray diffraction · 2 distinct chains · 28% helix, 32% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Ferredoxin--NADP reductase (EC 1.18.1.2) | protein | 247 | 28% helix, 33% strand | Q2T230 |
| B | Ferredoxin--NADP reductase (EC 1.18.1.2) | protein | 246 | 28% helix, 32% strand | Q2T230 |
Ligands and binding sites
- FAD · Flavin-adenine dinucleotide · ligand · 2 copies · chains A, B
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
5 pockets found on a 1 Å grid, 4 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 317 | 0.64 | 0.80 | 56 | empty |
| 2 | 176 | 0.58 | 0.81 | 22 | empty |
| 3 | 176 | 0.54 | 0.79 | 23 | FAD |
| 4 | 166 | 0.51 | 0.78 | 23 | FAD |
| 5 | 137 | 0.44 | 0.76 | 20 | empty |
Interfaces
1 interface between chains.
- A–B · 840 Ų buried · 12 hydrogen bonds · protein-protein
Compared structures
- 4FK8 · Crystal structure of FERREDOXIN-NADP REDUCTASE from burkholderia thailandensis E264 with… · 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 Q2T230
- Elsewhere: RCSB PDB 4FK8 · PDBe 4FK8 · UniProt Q2T230
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