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Crystal structure of the E. coli histidine kinase sensor TorS sensor domain

Analyse Crystal structure of the E. coli histidine kinase sensor TorS sensor domain in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 3I9W
Type: protein
Length: 270 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v2 / PDB Bank
Contract: 0xd58B01f6C18086e5202cdC5D7Ad3E41790360102
Owner: 0xF4e1AA6f26B7DA48EeAD9B24a97927303eeA07b8
Resolution: 2.7
Source: Escherichia coli K-12
Molecule: Sensor protein torS
EC: 2.7.13.3
UniProt: P39453
Pockets: 1 · best druggability 0.28

Structure

x-ray diffraction · resolution 2.7 · 1 distinct chain · 87% helix, 0% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Sensor protein torS (EC 2.7.13.3)	protein	270	87% helix, 0% strand	P39453

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	55	0.28	0.75	15	empty

Compared structures

3I9W · Crystal structure of the E. COLI histidine kinase sensor tors sensor domain · the same entry in another collection · chain A against A, TM-score 1.00
P39453 · AlphaFold monomer V2.0 prediction for sensor protein tors (P39453) · a predicted model of the same protein · chain A against A, TM-score 0.96

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 P39453
Elsewhere: RCSB PDB 3I9W · PDBe 3I9W · UniProt P39453

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