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Botulinum neurotoxin A4 hc domain

Analyse Botulinum neurotoxin A4 hc domain in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 6F0P
Type: protein
Length: 418 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Neurotoxin type a
UniProt: Q3LRX8
Ligands: NI
Pockets: 4 · best druggability 0.71

Structure

x-ray diffraction · 1 distinct chain · 6% helix, 46% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Neurotoxin type a	protein	418	6% helix, 46% strand	Q3LRX8

Ligands and binding sites

NI · Nickel (II) ion · metal · chains A
EDO · 1,2-ethanediol · additive · 5 copies · chains A
PEG · Di(hydroxyethyl)ether · additive · 2 copies · chains A
BTB · 2-[bis-(2-hydroxy-ethyl)-amino]-2-hydroxymethyl-propane-1,3-diol · additive · chains A

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

Pockets

4 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	397	0.71	0.83	38	EDO
2	140	0.49	0.79	23	empty
3	59	0.48	0.85	18	EDO
4	73	0.36	0.77	18	empty

Modifications

Observed in the structure: 1 disulfide (disulfide).

Compared structures

6F0P · Botulinum neurotoxin A4 Hc domain · 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 Q3LRX8
Elsewhere: RCSB PDB 6F0P · PDBe 6F0P · UniProt Q3LRX8

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