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Crystal structure of the catalytic domain of botulinum neurotoxin serotype a with an acetate ion bound at the active site

Analyse Crystal structure of the catalytic domain of botulinum neurotoxin serotype a… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 3BWI
Type: protein
Length: 423 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Botulinum neurotoxin a light chain
EC: 3.4.24.69
UniProt: A5HZZ9
Ligands: ZN, SO4
Pockets: 5 · best druggability 0.67

Structure

x-ray diffraction · 1 distinct chain · 30% helix, 18% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Botulinum neurotoxin a light chain (EC 3.4.24.69)	protein	423	30% helix, 18% strand	A5HZZ9

Ligands and binding sites

ZN · Zinc ion · metal · chains A
SO4 · Sulfate ion · ion · 2 copies · chains A
ACT · Acetate ion · additive · chains A

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

Pockets

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

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	439	0.67	0.79	37	ACT
2	75	0.34	0.75	16	empty
3	59	0.32	0.76	12	empty
4	54	0.31	0.77	14	empty
5	63	0.28	0.73	17	empty

Compared structures

3BWI · Crystal structure of the catalytic domain of botulinum neurotoxin serotype A with an… · 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 A5HZZ9
Elsewhere: RCSB PDB 3BWI · PDBe 3BWI · UniProt A5HZZ9

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