MolNFT v1 · #52366 · protein
FERREDOXIN:NADP reductase mutant with thr 155 replaced by gly, ala 160 replaced by thr, leu 263 replaced by pro and tyr 303 replaced by ser (T155G-A160T-L263P-Y303S)
2VYQ · Ferredoxin-NADP reductase: “FERREDOXIN:NADP reductase mutant with thr 155 replaced by gly, ala 160 replaced by thr, leu 263 replaced by…”. X-ray diffraction, 2 ligands (FAD, SO4), 2 pockets (best druggability 0.57). MolNFT v1 #52366…
- PDB
- 2VYQ
- 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 0.57
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 · 2 copies · 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 | 352 | 0.57 | 0.75 | 45 | FAD |
| 2 | 64 | 0.28 | 0.73 | 21 | GOL |
Compared structures
- 2VYQ · FERREDOXIN:NADP reductase mutant with thr 155 replaced by gly, ala 160 replaced by thr… · 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 2VYQ · PDBe 2VYQ · UniProt P21890
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