Research workbench

Structure of scorpion toxin variant-3 at 1.2 ångströms resolution

Analyse Structure of scorpion toxin variant-3 at 1.2 ångströms resolution in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 2SN3
Type: protein
Length: 65 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Scorpion neurotoxin (variant 3)
UniProt: P01494

Structure

x-ray diffraction · 1 distinct chain · 12% helix, 25% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Scorpion neurotoxin (variant 3)	protein	65	12% helix, 25% strand	P01494

Ligands and binding sites

MPD · (4S)-2-methyl-2,4-pentanediol · additive · chains A

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

Modifications

Observed in the structure: 4 disulfide (disulfide).

Compared structures

2SN3 · Structure of scorpion toxin variant-3 at 1.2 ångströms resolution · the same entry in another collection · chain A against A, TM-score 1.00
P01494 · AlphaFold monomer V2.0 prediction for toxin CSEV3 (P01494) · a predicted model of the same protein · chain A against A, TM-score 0.98

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 P01494
Elsewhere: RCSB PDB 2SN3 · PDBe 2SN3 · UniProt P01494

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