Research workbench
Ferredoxin NADP reductase mutant with glu 103 replaced by tyr, tyr 104 replaced by phe, ser 109 replaced by phe and gly 110 replaced by pro (E103Y-Y104F-S109F-G110P)
Analyse Ferredoxin NADP reductase mutant with glu 103 replaced by tyr, tyr 104 replaced… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 4C43
- Type
- protein
- Length
- 295 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
- P21890
- Ligands
- FAD, SO4
- Pockets
- 2 · best druggability 0.55
Structure
x-ray diffraction · 1 distinct chain · 27% helix, 29% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Ferredoxin--NADP reductase (EC 1.18.1.2) | protein | 295 | 27% helix, 29% strand | P21890 |
Ligands and binding sites
- FAD · Flavin-adenine dinucleotide · ligand · chains A
- SO4 · Sulfate ion · ion · chains A
- GOL · Glycerol · 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 | 231 | 0.55 | 0.78 | 31 | SO4 |
| 2 | 145 | 0.48 | 0.78 | 20 | FAD |
Compared structures
- 4C43 · Ferredoxin NADP reductase mutant with glu 103 replaced by tyr, tyr 104 replaced by phe… · the same entry in another collection · chain A against A, TM-score 1.00
- P21890 · AlphaFold monomer V2.0 prediction for ferredoxin--NADP reductase (P21890) · a predicted model of the same protein · chain A against A, TM-score 0.99
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 P21890
- Elsewhere: RCSB PDB 4C43 · PDBe 4C43 · UniProt P21890
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