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Ferredoxin-NADP reductase mutant with tyr 303 replaced by phe (Y303F)

Analyse Ferredoxin-NADP reductase mutant with tyr 303 replaced by phe (Y303F) in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 2X3U
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 0.52

Structure

x-ray diffraction · 1 distinct chain · 26% helix, 29% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Ferredoxin-NADP reductase (EC 1.18.1.2)	protein	295	26% 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.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	200	0.52	0.77	28	FAD
2	169	0.49	0.77	26	SO4

Compared structures

2X3U · Ferredoxin-NADP reductase mutant with Tyr 303 replaced by Phe (Y303F) · 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 2X3U · PDBe 2X3U · UniProt P21890

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