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Botulinum neurotoxin a light chain wt crystal form a

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

PDB: 2ISE
Type: protein
Length: 842 residues
Chains: 2
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Neurotoxin BONT/A
UniProt: Q7B8V4
Ligands: ZN
Pockets: 8 · best druggability 0.64

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	421	30% helix, 19% strand	Q7B8V4

Ligands and binding sites

ZN · Zinc ion · metal · 2 copies · chains A, B

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

Pockets

8 pockets found on a 1 Å grid, 4 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	473	0.64	0.77	47	empty
2	428	0.64	0.77	39	empty
3	93	0.53	0.84	16	empty
4	101	0.52	0.83	19	empty
5	73	0.33	0.75	12	empty

Interfaces

1 interface between chains.

A–B · 641 Å² buried · 12 hydrogen bonds · protein-protein

Compared structures

2ISE · Botulinum Neurotoxin A Light Chain WT Crystal Form A · 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 2ISE · PDBe 2ISE · UniProt Q7B8V4

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