Research workbench

Vegetative insecticidal protein 1 (VIP1AC1) from bacillus thuringiensis

Analyse Vegetative insecticidal protein 1 (VIP1AC1) from bacillus thuringiensis in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 6SMS
Type: protein
Length: 724 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Vegetative insecticidal protein 1AC from bacillus thuringiensis
Ligands: CA, SO4
Pockets: 11 · best druggability 0.48

Structure

x-ray diffraction · 1 distinct chain · 15% helix, 40% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Vegetative insecticidal protein 1AC from bacillus thuringiensis	protein	724	15% helix, 40% strand	—

Ligands and binding sites

CA · Calcium ion · metal · 3 copies · chains A
SO4 · Sulfate ion · ion · chains A
EDO · 1,2-ethanediol · additive · 3 copies · chains A

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

Pockets

11 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	193	0.48	0.75	28	empty
2	98	0.45	0.80	17	empty
3	127	0.45	0.77	25	empty
4	96	0.38	0.76	18	empty
5	57	0.37	0.79	18	empty

Modifications

Observed in the structure: 1 modified (oxidation).

Compared structures

6SMS · Vegetative Insecticidal Protein 1 (Vip1Ac1) from Bacillus thuringiensis · the same entry in another collection · chain A against A, TM-score 1.00

Analyse

Open in the research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides and crosslinks on the 3D structure
Elsewhere: RCSB PDB 6SMS · PDBe 6SMS

GL1X is a live explorer of the GenesisL1 blockchain. Turn on JavaScript for search, charts and interactive views.