MolNFT v1 · #51214 · protein

N- and C-terminal helices of oat LOV2 (404-546) are involved in light-induced signal transduction (cryo dark structure of LOV2 (404-546))

2V0U · NPH1-1: “N- and C-terminal helices of oat LOV2 (404-546) are involved in light-induced signal transduction (cryo dark…”. X-ray diffraction, 1 ligand (FMN), 1 pocket (best druggability 0.73). MolNFT v1 #51214 on GenesisL1: 3D…

PDB: 2V0U
Type: protein
Length: 146 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: NPH1-1
UniProt: O49003
Ligands: FMN
Pockets: 1 · best druggability 0.73

Structure

x-ray diffraction · 1 distinct chain · 36% helix, 27% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	NPH1-1	protein	146	36% helix, 27% strand	O49003

Ligands and binding sites

FMN · Flavin mononucleotide · ligand · chains A
GOL · Glycerol · additive · 6 copies · chains A

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

Pockets

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

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	160	0.73	0.91	23	FMN

Compared structures

2V0U · n- and c-terminal helices of oat lov2 (404-546) are involved in light-induced signal… · 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 O49003
Elsewhere: RCSB PDB 2V0U · PDBe 2V0U · UniProt O49003

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