MolNFT v1 · #95001 · protein

Structure of the fragaria X ananassa enone oxidoreductase in complex with NADPH and ehmf

4IDD · Ripening-induced protein: “Structure of the fragaria X ananassa enone oxidoreductase in complex with NADPH and ehmf”. X-ray diffraction, 3 ligands (NDP, 2XX, SO4), 2 pockets (best druggability 0.74). MolNFT v1 #95001 on GenesisL1…

PDB: 4IDD
Type: protein
Length: 321 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Ripening-induced protein
UniProt: O23939
Ligands: NDP, 2XX, SO4
Pockets: 2 · best druggability 0.74

Structure

x-ray diffraction · 1 distinct chain · 28% helix, 28% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Ripening-induced protein	protein	321	28% helix, 28% strand	O23939

Ligands and binding sites

NDP · Nadph dihydro-nicotinamide-adenine-dinucleotide phosphate · ligand · chains A
2XX · (2R)-2-ethyl-4-hydroxy-5-methylfuran-3(2H)-one · ligand · chains A
SO4 · Sulfate ion · ion · chains A
EDO · 1,2-ethanediol · 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.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	496	0.74	0.82	51	NDP, 2XX
2	67	0.31	0.75	18	empty

Compared structures

4IDD · Structure of the Fragaria x ananassa e oxidoreductase in complex with NADPH and EHMF · 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 O23939
Elsewhere: RCSB PDB 4IDD · PDBe 4IDD · UniProt O23939

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