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Structure of BoNT mutant

Analyse Structure of BoNT mutant in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 6MHJ
Type: protein
Length: 322 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v2 / PDB Bank
Contract: 0xd58B01f6C18086e5202cdC5D7Ad3E41790360102
Owner: 0xF4e1AA6f26B7DA48EeAD9B24a97927303eeA07b8
Resolution: 3.019
Source: Clostridium botulinum A str. ATCC 19397
Molecule: Botulinum neurotoxin type A
EC: 3.4.24.69
UniProt: P0DPI0
Ligands: PO4
Pockets: 2 · best druggability 0.42

Structure

x-ray diffraction · resolution 3.019 · 1 distinct chain · 67% helix, 2% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Botulinum neurotoxin type A (EC 3.4.24.69)	protein	322	67% helix, 2% strand	P0DPI0

Ligands and binding sites

PO4 · Phosphate ion · ion · 9 copies · chains A

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

Pockets

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

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	60	0.42	0.82	15	empty
2	55	0.31	0.76	12	empty

Compared structures

6MHJ · Structure of bont mutant · the same entry in another collection · chain A against A, TM-score 1.00
P0DPI0 · AlphaFold monomer V2.0 prediction for botulinum neurotoxin type a (P0DPI0) · 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 P0DPI0
Elsewhere: RCSB PDB 6MHJ · PDBe 6MHJ · UniProt P0DPI0

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