Research workbench

The crystal structure of the oxidoreductase containing FMN

Analyse The crystal structure of the oxidoreductase containing FMN in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 2FRE
Type: protein
Length: 398 residues
Chains: 2
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: NAD(P)H-flavin oxidoreductase
UniProt: Q8UJB5
Ligands: FMN
Pockets: 3 · best druggability 0.62

Structure

x-ray diffraction · 2 distinct chains · 34% helix, 24% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	NAD(P)H-flavin oxidoreductase	protein	200	34% helix, 24% strand	Q8UJB5
B	NAD(P)H-flavin oxidoreductase	protein	198	34% helix, 24% strand	Q8UJB5

Ligands and binding sites

FMN · Flavin mononucleotide · ligand · 2 copies · chains A, B

Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.

Pockets

3 pockets found on a 1 Å grid, 2 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	326	0.62	0.79	51	FMN
2	212	0.57	0.79	29	FMN
3	107	0.39	0.76	25	empty

Interfaces

1 interface between chains.

A–B · 3386 Å² buried · 45 hydrogen bonds · protein-protein

Modifications

Observed in the structure: 10 modified (engineered).

Compared structures

2FRE · The crystal structure of the oxidoreductase containing FMN · 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 Q8UJB5
Elsewhere: RCSB PDB 2FRE · PDBe 2FRE · UniProt Q8UJB5

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