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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 v2 / PDB Bank
Contract: 0xd58B01f6C18086e5202cdC5D7Ad3E41790360102
Owner: 0xF4e1AA6f26B7DA48EeAD9B24a97927303eeA07b8
Resolution: 1.2
Source: Centruroides exilicauda
Molecule: Scorpion neurotoxin (variant 3)
UniProt: P01494

Structure

x-ray diffraction · resolution 1.2 · 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

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