Research workbench

Tetanus neurotoxin translocation domain -C467S

Analyse Tetanus neurotoxin translocation domain -C467S in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 7BXX
Type: protein
Length: 592 residues
Chains: 2
Method: x-ray diffraction; solution scattering
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Tetanus toxin
EC: 3.4.24.68
UniProt: P04958
Pockets: 3 · best druggability 0.54

Structure

x-ray diffraction; solution scattering · 2 distinct chains · 65% helix, 2% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Tetanus toxin (EC 3.4.24.68)	protein	301	65% helix, 3% strand	P04958
B	Tetanus toxin (EC 3.4.24.68)	protein	291	66% helix, 2% strand	P04958

Pockets

3 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	322	0.54	0.75	49	empty
2	87	0.35	0.74	25	empty
3	57	0.28	0.74	14	empty

Interfaces

1 interface between chains.

A–B · 485 Å² buried · 6 hydrogen bonds · protein-protein

Compared structures

7BXX · Tetanus neurotoxin translocation domain -C467S · the same entry in another collection · chain A against A, TM-score 1.00
P04958 · AlphaFold monomer V2.0 prediction for tetanus toxin (P04958) · a predicted model of the same protein · chain A against A, TM-score 0.97

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 P04958
Elsewhere: RCSB PDB 7BXX · PDBe 7BXX · UniProt P04958

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