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Plasticity of pas domain and potential role for signal transduction in the histidine-kinase dcus

Analyse Plasticity of pas domain and potential role for signal transduction in the… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB
2W0N
Type
protein
Length
118 residues
Chains
1
Method
solid-state nmr
Collection
MolNFT v1 / PDB
Contract
0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner
0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule
Sensor protein dcus
EC
2.7.13.3
UniProt
P0AEC8
Pockets
2 · best druggability 0.53

Structure

solid-state nmr · 1 distinct chain · 24% helix, 13% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
ASensor protein dcus (EC 2.7.13.3)protein11824% helix, 13% strandP0AEC8

Pockets

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

PocketVolume (ų)DruggabilityBuriednessLining residuesInside
11130.530.8221empty
21590.450.7623empty

Compared structures

  • 2W0N · Plasticity of PAS domain and potential role for signal transduction in the… · the same entry in another collection · chain A against A, TM-score 1.00
  • P0AEC8 · AlphaFold monomer V2.0 prediction for sensor histidine kinase dcus (P0AEC8) · a predicted model of the same protein · chain A against A, TM-score 0.43

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