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Crystal structure of toxic effector TSE1

Analyse Crystal structure of toxic effector TSE1 in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 4FQA
Type: protein
Length: 155 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Toxic effector TSE1
UniProt: Q9I2Q1
Pockets: 1 · best druggability 0.35

Structure

x-ray diffraction · 1 distinct chain · 34% helix, 20% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Toxic effector TSE1	protein	155	34% helix, 20% strand	Q9I2Q1

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	95	0.35	0.74	24	empty

Modifications

Observed in the structure: 1 disulfide (disulfide).

Compared structures

4FQA · Crystal structure of toxic effector Tse1 · the same entry in another collection · chain A against A, TM-score 1.00
Q9I2Q1 · AlphaFold monomer V2.0 prediction for peptidoglycan amidase TSE1 (Q9I2Q1) · a predicted model of the same protein · chain A against A, TM-score 0.97

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Open in the research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides and crosslinks on the 3D structure
Every structure of UniProt Q9I2Q1
Elsewhere: RCSB PDB 4FQA · PDBe 4FQA · UniProt Q9I2Q1

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