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Tetanus toxin C fragment

Analyse Tetanus toxin C fragment in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 1A8D
Type: protein
Length: 452 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Tetanus neurotoxin
EC: 3.4.24.68
UniProt: P04958
Ligands: AU
Pockets: 5 · best druggability 0.49

Structure

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

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Tetanus neurotoxin (EC 3.4.24.68)	protein	452	8% helix, 45% strand	P04958

Ligands and binding sites

AU · Gold ion · metal · 2 copies · chains A

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

Pockets

5 pockets found on a 1 Å grid, 0 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	157	0.49	0.78	23	empty
2	69	0.38	0.79	15	empty
3	93	0.34	0.75	19	empty
4	76	0.32	0.74	19	empty
5	51	0.26	0.74	14	empty

Modifications

Observed in the structure: 1 disulfide (disulfide).

Compared structures

1A8D · Tetanus toxin C fragment · 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 0.98

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 1A8D · PDBe 1A8D · UniProt P04958

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