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Inactive mutant toxic shock syndrome toxin-1 at 2.5 a

Analyse Inactive mutant toxic shock syndrome toxin-1 at 2.5 a in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 1QIL
Type: protein
Length: 582 residues
Chains: 3
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Toxic shock syndrome toxin-1
UniProt: P06886
Pockets: 6 · best druggability 0.79

Structure

x-ray diffraction · 1 distinct chain · 16% helix, 46% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A, B, C	Toxic shock syndrome toxin-1	protein	194	16% helix, 46% strand	P06886

Pockets

6 pockets found on a 1 Å grid, 2 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	1103	0.79	0.80	73	empty
2	337	0.65	0.80	33	empty
3	66	0.35	0.77	15	empty
4	62	0.33	0.76	13	empty
5	86	0.33	0.74	25	empty

Interfaces

2 interfaces between chains.

A–C · 1264 Å² buried · 23 hydrogen bonds · protein-protein
A–B · 269 Å² buried · 3 hydrogen bonds · protein-protein

Compared structures

1QIL · Inactive mutant toxic shock syndrome toxin-1 at 2.5 a · the same entry in another collection · chain A against A, TM-score 1.00
P06886 · AlphaFold monomer V2.0 prediction for toxic shock syndrome toxin-1 (P06886) · 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 P06886
Elsewhere: RCSB PDB 1QIL · PDBe 1QIL · UniProt P06886

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