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Structure of succinyl-CoA: 3-ketoacid CoA transferase from drosophila melanogaster

Analyse Structure of succinyl-CoA: 3-ketoacid CoA transferase from drosophila… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB
4KGB
Type
protein
Length
930 residues
Chains
2
Method
x-ray diffraction
Collection
MolNFT v1 / PDB
Contract
0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner
0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule
Succinyl-COA:3-ketoacid-coenzyme a transferase
EC
2.8.3.5
UniProt
Q9W058
Ligands
SO4
Pockets
9 · best druggability 0.84

Structure

x-ray diffraction · 2 distinct chains · 22% helix, 31% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
ASuccinyl-COA:3-ketoacid-coenzyme a transferase (EC 2.8.3.5)protein46622% helix, 31% strandQ9W058
BSuccinyl-COA:3-ketoacid-coenzyme a transferase (EC 2.8.3.5)protein46422% helix, 31% strandQ9W058

Ligands and binding sites

  • SO4 · Sulfate ion · ion · chains B

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

Pockets

9 pockets found on a 1 Å grid, 6 with a druggability of 0.5 or more.

PocketVolume (ų)DruggabilityBuriednessLining residuesInside
13170.840.9445empty
25370.700.8082empty
34250.670.8062empty
42200.620.8138empty
53770.600.7659empty

Interfaces

1 interface between chains.

  • A–B · 2229 Ų buried · 27 hydrogen bonds · protein-protein

Compared structures

  • 4KGB · Structure of succinyl-CoA: 3-ketoacid CoA transferase from Drosophila melanogaster · the same entry in another collection · chain A against A, TM-score 1.00
  • Q9W058 · AlphaFold monomer V2.0 prediction for succinyl-COA:3-ketoacid- coenzyme a transferase… · a predicted model of the same protein · chain B against A, TM-score 0.99

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