Research workbench

Crystal structure of botulinum neurotoxin serotype D binding domain

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

PDB: 3OBR
Type: protein
Length: 418 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Botulinum neurotoxin type D
EC: 3.4.24.69
UniProt: P19321
Pockets: 4 · best druggability 0.75

Structure

x-ray diffraction · 1 distinct chain · 7% helix, 43% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Botulinum neurotoxin type D (EC 3.4.24.69)	protein	418	7% helix, 43% strand	P19321

Ligands and binding sites

GOL · Glycerol · additive · 10 copies · 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, 2 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	178	0.75	0.91	31	empty
2	68	0.52	0.86	16	GOL
3	68	0.41	0.80	19	empty
4	84	0.34	0.75	16	empty

Modifications

Observed in the structure: 1 disulfide (disulfide).

Compared structures

3OBR · Crystal structure of Botulinum neurotoxin serotype D binding 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 P19321
Elsewhere: RCSB PDB 3OBR · PDBe 3OBR · UniProt P19321

GL1X is a live explorer of the GenesisL1 blockchain. Turn on JavaScript for search, charts and interactive views.