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N-terminal helix reorients in recombinant C-fragment of clostridium botulinum type B

Analyse N-terminal helix reorients in recombinant C-fragment of clostridium botulinum… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 1Z0H
Type: protein
Length: 876 residues
Chains: 2
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Botulinum neurotoxin type B
EC: 3.4.24.69
UniProt: P10844
Pockets: 8 · best druggability 0.66

Structure

x-ray diffraction · 1 distinct chain · 8% helix, 45% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A, B	Botulinum neurotoxin type B (EC 3.4.24.69)	protein	438	8% helix, 45% strand	P10844

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	329	0.66	0.81	44	empty
2	298	0.62	0.79	37	empty
3	96	0.60	0.88	23	empty
4	105	0.60	0.87	23	empty
5	109	0.39	0.76	16	empty

Compared structures

1Z0H · N-terminal helix reorients in recombinant C-fragment of Clostridium botulinum type B · the same entry in another collection · chain A against A, TM-score 1.00
P10844 · AlphaFold monomer V2.0 prediction for botulinum neurotoxin type B (P10844) · a predicted model of the same protein · chain A against A, TM-score 0.95

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 P10844
Elsewhere: RCSB PDB 1Z0H · PDBe 1Z0H · UniProt P10844

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