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Botulinum neurotoxin a light chain wt crystal form B

Analyse Botulinum neurotoxin a light chain wt crystal form B in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 2ISG
Type: protein
Length: 832 residues
Chains: 2
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Neurotoxin BONT/A
UniProt: Q7B8V4
Ligands: ZN, NI
Pockets: 12 · best druggability 0.72

Structure

x-ray diffraction · 1 distinct chain · 30% helix, 19% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A, B	Neurotoxin BONT/A	protein	416	30% helix, 19% strand	Q7B8V4

Ligands and binding sites

ZN · Zinc ion · metal · 2 copies · chains A, B
NI · Nickel (II) ion · metal · 2 copies · chains B, A

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

Pockets

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

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	809	0.72	0.77	66	empty
2	370	0.66	0.80	35	empty
3	63	0.40	0.80	16	empty
4	95	0.35	0.74	20	empty
5	59	0.34	0.77	13	empty

Interfaces

1 interface between chains.

A–B · 626 Å² buried · 5 hydrogen bonds · protein-protein

Compared structures

2ISG · Botulinum Neurotoxin A Light Chain WT Crystal Form B · 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 Q7B8V4
Elsewhere: RCSB PDB 2ISG · PDBe 2ISG · UniProt Q7B8V4

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