Research workbench
Crystal structure of the FERREDOXIN:NADP+ reductase from maize root at 1.7 ångströms - test set withheld
Analyse Crystal structure of the FERREDOXIN:NADP+ reductase from maize root at 1.7… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 3LVB
- Type
- protein
- Length
- 311 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Ferredoxin-NADP reductase
- EC
- 1.18.1.2
- UniProt
- Q41736
- Ligands
- FAD
- Pockets
- 1 · best druggability 0.61
Structure
x-ray diffraction · 1 distinct chain · 28% helix, 27% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Ferredoxin-NADP reductase (EC 1.18.1.2) | protein | 311 | 28% helix, 27% strand | Q41736 |
Ligands and binding sites
- FAD · Flavin-adenine dinucleotide · ligand · 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 | 349 | 0.61 | 0.78 | 43 | FAD |
Modifications
Observed in the structure: 1 disulfide (disulfide).
Compared structures
- 3LVB · Crystal structure of the Ferredoxin:NADP+ reductase from maize root at 1.7 angstroms… · 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 Q41736
- Elsewhere: RCSB PDB 3LVB · PDBe 3LVB · UniProt Q41736
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