Research workbench
X-ray structure of the ferredoxin-NADP(H) reductase from rhodobacter capsulatus in complex with NADP. form II at 2.27 ångströms resolution
Analyse X-ray structure of the ferredoxin-NADP(H) reductase from rhodobacter capsulatus… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 2VNH
- Type
- protein
- Length
- 260 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v2 / PDB Bank
- Contract
- 0xd58B01f6C18086e5202cdC5D7Ad3E41790360102
- Owner
- 0xF4e1AA6f26B7DA48EeAD9B24a97927303eeA07b8
- Resolution
- 2.27
- Source
- RHODOBACTER CAPSULATUS
- Molecule
- NADPH\:FERREDOXIN reductase
- EC
- 1.18.1.2
- UniProt
- Q9L6V3
- Ligands
- FAD, NAP
- Pockets
- 1 · best druggability 0.66
Structure
x-ray diffraction · resolution 2.27 · 1 distinct chain · 22% helix, 30% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | NADPH\:FERREDOXIN reductase (EC 1.18.1.2) | protein | 260 | 22% helix, 30% strand | Q9L6V3 |
Ligands and binding sites
- FAD · Flavin-adenine dinucleotide · ligand · chains A
- NAP · Nadp nicotinamide-adenine-dinucleotide phosphate · ligand · chains A
- HTG · heptyl 1-thio-beta-D-glucopyranoside · additive · chains A
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
1 pocket found on a 1 Å grid, 1 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 385 | 0.66 | 0.79 | 46 | FAD, NAP |
Compared structures
- 2VNH · X-ray structure of the ferredoxin-NADP(H) reductase from rhodobacter capsulatus in… · the same entry in another collection · chain A against A, TM-score 1.00
- Q9L6V3 · AlphaFold monomer V2.0 prediction for FLAVODOXIN/FERREDOXIN--NADP reductase (Q9L6V3) · a predicted model of the same protein · chain A against A, TM-score 0.98
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 Q9L6V3
- Elsewhere: RCSB PDB 2VNH · PDBe 2VNH · UniProt Q9L6V3
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