Research workbench

NADH:FMN oxidoreductase from paracoccus denitrificans

Analyse NADH:FMN oxidoreductase from paracoccus denitrificans in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 4XHY
Type: protein
Length: 161 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Flavin reductase domain protein, FMN-binding protein
UniProt: A1B5I2
Pockets: 1 · best druggability 0.41

Structure

x-ray diffraction · 1 distinct chain · 12% helix, 41% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Flavin reductase domain protein, FMN-binding protein	protein	161	12% helix, 41% strand	A1B5I2

Pockets

1 pocket found on a 1 Å grid, 0 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	141	0.41	0.74	30	empty

Compared structures

4XHY · NADH:FMN oxidoreductase from Paracoccus denitrificans · 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 A1B5I2
Elsewhere: RCSB PDB 4XHY · PDBe 4XHY · UniProt A1B5I2

GL1X is a live explorer of the GenesisL1 blockchain. Turn on JavaScript for search, charts and interactive views.