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Chey-binding domain of chea in complex with chey from crystals soaked in acetyl phosphate

Analyse Chey-binding domain of chea in complex with chey from crystals soaked in acetyl… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB
1FFS
Type
protein
Length
392 residues
Chains
4
Method
x-ray diffraction
Collection
MolNFT v1 / PDB
Contract
0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner
0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule
Chemotaxis protein chey; Chemotaxis protein chea
EC
2.7.3.-
UniProt
P06143, P07363
Ligands
MN
Pockets
5 · best druggability 0.49

Structure

x-ray diffraction · 2 distinct chains · 40% helix, 21% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
A, CChemotaxis protein chey (EC 2.7.3.-)protein12843% helix, 17% strandP06143
B, DChemotaxis protein cheaprotein6834% helix, 29% strandP07363

Ligands and binding sites

  • MN · Manganese (II) ion · metal · 2 copies · chains A, C

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

Pockets

5 pockets found on a 1 Å grid, 0 with a druggability of 0.5 or more.

PocketVolume (ų)DruggabilityBuriednessLining residuesInside
11940.490.7628empty
21410.470.7723empty
31480.450.7625empty
4550.290.7511empty
5630.280.7313empty

Interfaces

3 interfaces between chains.

  • C–D · 623 Ų buried · 7 hydrogen bonds · protein-protein
  • A–B · 616 Ų buried · 7 hydrogen bonds · protein-protein
  • A–C · 220 Ų buried · 3 hydrogen bonds · protein-protein

Compared structures

  • 1FFS · Chey-binding domain of chea in complex with chey from crystals soaked in acetyl phosphate · the same entry in another collection · chain A against A, TM-score 1.00
  • P07363 · AlphaFold monomer V2.0 prediction for chemotaxis protein chea (P07363) · a predicted model of the same protein · chain D against A, TM-score 0.97

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