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Ketosynthase (apeo) in complex with its chain length factor (apec) from xenorhabdus doucetiae

Analyse Ketosynthase (apeo) in complex with its chain length factor (apec) from… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB
6QSP
Type
protein
Length
637 residues
Chains
2
Method
x-ray diffraction
Collection
MolNFT v1 / PDB
Contract
0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner
0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule
Beta-ketoacyl synthase; Uncharacterized protein
EC
2.3.1.41
UniProt
A0A068QVX9, A0A068QZ94
Ligands
PO4
Pockets
7 · best druggability 0.78

Structure

x-ray diffraction · 2 distinct chains · 38% helix, 24% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
ABeta-ketoacyl synthase (EC 2.3.1.41)protein39938% helix, 23% strandA0A068QVX9
BUncharacterized proteinprotein23837% helix, 26% strandA0A068QZ94

Ligands and binding sites

  • PO4 · Phosphate ion · ion · chains B
  • GOL · Glycerol · additive · 4 copies · chains A, B

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

Pockets

7 pockets found on a 1 Å grid, 4 with a druggability of 0.5 or more.

PocketVolume (ų)DruggabilityBuriednessLining residuesInside
11060.780.9729empty
2690.760.9922GOL
31320.650.8725empty
42540.630.8138empty
5720.300.7320empty

Interfaces

1 interface between chains.

  • A–B · 2338 Ų buried · 26 hydrogen bonds · protein-protein

Compared structures

  • 6QSP · Ketosynthase (ApeO) in Complex with its Chain Length Factor (ApeC) from Xenorhabdus… · the same entry in another collection · chain A against A, TM-score 1.00

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