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Room temperature structure of the LOV2 domain of phototropin-2 from arabidopsis thaliana 4158 ms after initiation of illumination, determined with a serial crystallography approach

Analyse Room temperature structure of the LOV2 domain of phototropin-2 from arabidopsis… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 6S46
Type: protein
Length: 116 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Phototropin-2
EC: 2.7.11.1
UniProt: P93025
Ligands: FMN
Pockets: 1 · best druggability 0.72

Structure

x-ray diffraction · 1 distinct chain · 27% helix, 34% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Phototropin-2 (EC 2.7.11.1)	protein	116	27% helix, 34% strand	P93025

Ligands and binding sites

FMN · Flavin mononucleotide · ligand · 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	192	0.72	0.89	25	FMN

Compared structures

6S46 · Room temperature structure of the LOV2 domain of phototropin-2 from Arabidopsis thaliana… · the same entry in another collection · chain A against A, TM-score 1.00
P93025 · AlphaFold monomer V2.0 prediction for phototropin-2 (P93025) · a predicted model of the same protein · chain A against A, TM-score 0.93

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 P93025
Elsewhere: RCSB PDB 6S46 · PDBe 6S46 · UniProt P93025

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