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E. COLI core signaling unit, carrying qqqq receptor mutation

Analyse E. COLI core signaling unit, carrying qqqq receptor mutation in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB
6S1K
Type
protein
Length
2,280 residues
Chains
16
Method
electron microscopy
Collection
MolNFT v1 / PDB
Contract
0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner
0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule
Chemotaxis protein chea; Chew; Methyl-accepting chemotaxis protein I
EC
2.7.13.3
UniProt
P07363, P02942
Pockets
20 · best druggability 0.80

Structure

electron microscopy · 3 distinct chains · 43% helix, 30% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
A, BChemotaxis protein chea (EC 2.7.13.3)protein38339% helix, 30% strandP07363
C, DChewprotein14519% helix, 50% strand—
E, F, G, H, I, J, K, L, M, N, O, PMethyl-accepting chemotaxis protein Iprotein10296% helix, 0% strandP02942

Pockets

20 pockets found on a 1 Å grid, 16 with a druggability of 0.5 or more.

PocketVolume (ų)DruggabilityBuriednessLining residuesInside
111950.800.81117empty
28250.790.8286empty
311760.750.78116empty
4730.730.9720empty
511230.730.7694empty

Interfaces

27 interfaces between chains.

  • M–N · 2160 Ų buried · 4 hydrogen bonds · protein-protein
  • O–P · 2099 Ų buried · 4 hydrogen bonds · protein-protein
  • G–H · 2095 Ų buried · 7 hydrogen bonds · protein-protein
  • E–F · 2043 Ų buried · 3 hydrogen bonds · protein-protein
  • I–J · 2023 Ų buried · 2 hydrogen bonds · protein-protein

Compared structures

  • 6S1K · E. coli Core Signaling Unit, carrying QQQQ receptor mutation · the same entry in another collection · chain P against P, TM-score 1.00

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