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Crystal structure of the catalytic domain of alpha-toxin from clostridium novyi

Analyse Crystal structure of the catalytic domain of alpha-toxin from clostridium novyi in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 2VK9
Type: protein
Length: 540 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Alpha-toxin
UniProt: Q46149
Pockets: 2 · best druggability 0.74

Structure

x-ray diffraction · 1 distinct chain · 56% helix, 8% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Alpha-toxin	protein	540	56% helix, 8% strand	Q46149

Pockets

2 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	956	0.74	0.78	79	empty
2	89	0.37	0.76	21	empty

Compared structures

2VK9 · Crystal structure of the catalytic domain of alpha-toxin from clostridium novyi · the same entry in another collection · chain A against A, TM-score 1.00
Q46149 · AlphaFold monomer V2.0 prediction for toxin a (Q46149) · a predicted model of the same protein · chain A against A, TM-score 0.99

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 Q46149
Elsewhere: RCSB PDB 2VK9 · PDBe 2VK9 · UniProt Q46149

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