Research workbench

Crystal structure of the lhn fragment of botulinum neurotoxin type D, mutant H233Y E230Q

Analyse Crystal structure of the lhn fragment of botulinum neurotoxin type D, mutant… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 5BQN
Type: protein
Length: 838 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Botulinum neurotoxin type D,BOTULINUM neurotoxin type D
EC: 3.4.24.69
UniProt: P19321
Pockets: 10 · best druggability 0.83

Structure

x-ray diffraction · 1 distinct chain · 41% helix, 14% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Botulinum neurotoxin type D,BOTULINUM neurotoxin type D (EC 3.4.24.69)	protein	838	41% helix, 14% strand	P19321

Ligands and binding sites

EPE · 4-(2-hydroxyethyl)-1-piperazine ethanesulfonic acid · additive · chains A

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

Pockets

10 pockets found on a 1 Å grid, 6 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	832	0.83	0.85	108	empty
2	459	0.67	0.79	44	empty
3	459	0.66	0.78	45	empty
4	93	0.63	0.89	22	empty
5	356	0.59	0.77	38	empty

Modifications

Observed in the structure: 1 disulfide (disulfide).

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 5BQN · PDBe 5BQN · UniProt P19321

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