Research workbench
X-ray structure of the ferredoxin-NADP(H) reductase from rhodobacter capsulatus in complex with 2P-AMP at 2.37 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
- 2VNI
- Type
- protein
- Length
- 257 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- NADPH\:FERREDOXIN reductase
- EC
- 1.18.1.2
- UniProt
- Q9L6V3
- Ligands
- FAD, A2P
- Pockets
- 2 · best druggability 0.70
Structure
x-ray diffraction · 1 distinct chain · 25% helix, 34% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | NADPH\:FERREDOXIN reductase (EC 1.18.1.2) | protein | 257 | 25% helix, 34% strand | Q9L6V3 |
Ligands and binding sites
- FAD · Flavin-adenine dinucleotide · ligand · chains A
- A2P · Adenosine-2'-5'-diphosphate · 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
2 pockets found on a 1 Å grid, 1 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 474 | 0.70 | 0.80 | 45 | FAD, A2P |
| 2 | 86 | 0.33 | 0.74 | 22 | empty |
Compared structures
- 2VNI · 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 2VNI · PDBe 2VNI · UniProt Q9L6V3
GL1X is a live explorer of the GenesisL1 blockchain. Turn on JavaScript for search, charts and interactive views.