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Crystal structure of the water-soluble state of the pore-forming cytolysin sticholysin II complexed with glycerol

Analyse Crystal structure of the water-soluble state of the pore-forming cytolysin… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 1O71
Type: protein
Length: 350 residues
Chains: 2
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Sticholysin II
UniProt: P07845
Pockets: 1 · best druggability 0.31

Structure

x-ray diffraction · 1 distinct chain · 12% helix, 47% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A, B	Sticholysin II	protein	175	12% helix, 47% strand	P07845

Ligands and binding sites

GOL · Glycerol · additive · 6 copies · chains A, B

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

Pockets

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

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	54	0.31	0.76	17	empty

Interfaces

1 interface between chains.

A–B · 372 Å² buried · 3 hydrogen bonds · protein-protein

Compared structures

1O71 · Crystal structure of the water-soluble state of the pore-forming cytolysin Sticholysin II… · the same entry in another collection · chain A against A, TM-score 1.00
P07845 · AlphaFold monomer V2.0 prediction for delta-stichotoxin-SHE4B (P07845) · a predicted model of the same protein · chain B 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 P07845
Elsewhere: RCSB PDB 1O71 · PDBe 1O71 · UniProt P07845

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