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Fructose binding periplasmic domain of hybrid two component system BT1754

Analyse Fructose binding periplasmic domain of hybrid two component system BT1754 in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB
2X7X
Type
protein
Length
601 residues
Chains
2
Method
x-ray diffraction
Collection
MolNFT v1 / PDB
Contract
0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner
0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule
Sensor protein
EC
2.7.13.3
UniProt
Q8A6X1
Ligands
FRU, K, PO4
Pockets
2 · best druggability 0.66

Structure

x-ray diffraction · 2 distinct chains · 46% helix, 21% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
ASensor protein (EC 2.7.13.3)protein30146% helix, 21% strandQ8A6X1
BSensor protein (EC 2.7.13.3)protein30046% helix, 21% strandQ8A6X1

Ligands and binding sites

  • FRU · beta-D-fructofuranose · sugar · 2 copies · chains A, B
  • K · Potassium ion · metal · 3 copies · chains A, B
  • PO4 · Phosphate ion · ion · 4 copies · chains A, B

Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.

Pockets

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

PocketVolume (ų)DruggabilityBuriednessLining residuesInside
12930.660.8236PO4
22700.650.8240PO4

Interfaces

1 interface between chains.

  • A–B · 1368 Ų buried · 4 hydrogen bonds · protein-protein

Compared structures

  • 2X7X · Fructose binding periplasmic domain of hybrid two component system BT1754 · the same entry in another collection · chain A against A, TM-score 1.00

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