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Proton nuclear magnetic resonance and distance GEOMETRY(SLASH) simulated annealing studies on the variant-1 neurotoxin from the new world scorpion centruroides sculpturatus ewing

Analyse Proton nuclear magnetic resonance and distance GEOMETRY(SLASH) simulated… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 1VNB
Type: protein
Length: 65 residues
Chains: 1
Method: solution nmr
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Neurotoxin
UniProt: P01492
Pockets: 1 · best druggability 0.31

Structure

solution nmr · 1 distinct chain · 9% helix, 28% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Neurotoxin	protein	65	9% helix, 28% strand	P01492

Pockets

1 pocket found on a 1 Å grid, 0 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	63	0.31	0.75	16	empty

Modifications

Observed in the structure: 4 disulfide (disulfide).

Compared structures

1VNB · Proton nuclear magnetic resonance and distance GEOMETRY(SLASH)SIMULATED annealing studies… · the same entry in another collection · chain A against A, TM-score 1.00
P01492 · AlphaFold monomer V2.0 prediction for toxin CSEV1 (P01492) · a predicted model of the same protein · chain A against A, TM-score 0.82

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 P01492
Elsewhere: RCSB PDB 1VNB · PDBe 1VNB · UniProt P01492

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