MolNFT v1 · #135344 · protein
Oxidoreductase iruo in the oxidized form
5TWC · Ferredoxin--NADP reductase: “Oxidoreductase iruo in the oxidized form”. X-ray diffraction, 1 ligand (FAD), 1 pocket (best druggability 0.74). MolNFT v1 #135344 on GenesisL1: 3D structure, binding sites and pockets in GL1X.
- PDB
- 5TWC
- Type
- protein
- Length
- 344 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
- Q2FEC4
- Ligands
- FAD
- Pockets
- 1 · best druggability 0.74
Structure
x-ray diffraction · 1 distinct chain · 27% helix, 26% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Ferredoxin--NADP reductase (EC 1.18.1.2) | protein | 344 | 27% helix, 26% strand | Q2FEC4 |
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 | 702 | 0.74 | 0.80 | 86 | FAD |
Modifications
Observed in the structure: 1 disulfide (disulfide).
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 Q2FEC4
- Elsewhere: RCSB PDB 5TWC · PDBe 5TWC · UniProt Q2FEC4
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