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Cell entry of botulinum neurotoxin type C is dependent upon interaction with two ganglioside molecules

Analyse Cell entry of botulinum neurotoxin type C is dependent upon interaction with… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 3R4U
Type: protein
Length: 844 residues
Chains: 2
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Botulinum neurotoxin type C1
EC: 3.4.24.69
UniProt: P18640
Pockets: 7 · best druggability 0.63

Structure

x-ray diffraction · 1 distinct chain · 9% helix, 49% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A, B	Botulinum neurotoxin type C1 (EC 3.4.24.69)	protein	422	9% helix, 49% strand	P18640

Pockets

7 pockets found on a 1 Å grid, 3 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	487	0.63	0.76	46	empty
2	510	0.63	0.75	53	empty
3	220	0.54	0.78	38	empty
4	105	0.46	0.79	26	empty
5	99	0.36	0.75	17	empty

Interfaces

1 interface between chains.

A–B · 805 Å² buried · 13 hydrogen bonds · protein-protein

Compared structures

3R4U · Cell entry of botulinum neurotoxin type C is dependent upon interaction with two… · the same entry in another collection · chain A against A, TM-score 1.00

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 P18640
Elsewhere: RCSB PDB 3R4U · PDBe 3R4U · UniProt P18640

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