MolNFT v1 · #104893 · protein

Crystal structure of FMN quinone reductase 2 at 1.55A

4QOF · Ribosyldihydronicotinamide dehydrogenase [quinone]: “Crystal structure of FMN quinone reductase 2 at 1.55A”. X-ray diffraction, 2 ligands (FMN, ZN), 2 pockets (best druggability 0.79). MolNFT v1 #104893 on GenesisL1: 3D structure…

PDB: 4QOF
Type: protein
Length: 456 residues
Chains: 2
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Ribosyldihydronicotinamide dehydrogenase [quinone]
EC: 1.10.99.2
UniProt: P16083
Ligands: FMN, ZN
Pockets: 2 · best druggability 0.79

Structure

x-ray diffraction · 1 distinct chain · 41% helix, 16% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A, B	Ribosyldihydronicotinamide dehydrogenase [quinone] (EC 1.10.99.2)	protein	228	41% helix, 16% strand	P16083

Ligands and binding sites

FMN · Flavin mononucleotide · ligand · 2 copies · chains A, B
ZN · Zinc ion · metal · 2 copies · chains A, B

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

Pockets

2 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	551	0.79	0.85	47	FMN
2	590	0.77	0.83	47	FMN

Interfaces

1 interface between chains.

A–B · 2060 Å² buried · 32 hydrogen bonds · protein-protein

Compared structures

4QOF · Crystal structure of fmn qui reductase 2 AT 1.55A · 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 P16083
Elsewhere: RCSB PDB 4QOF · PDBe 4QOF · UniProt P16083

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