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Crystal structure of phosphorylated pig heart, GTP-specific succinyl- CoA synthetase

Analyse Crystal structure of phosphorylated pig heart, GTP-specific succinyl- CoA… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB
1EUD
Type
protein
Length
701 residues
Chains
2
Method
x-ray diffraction
Collection
MolNFT v1 / PDB
Contract
0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner
0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule
Succinyl-CoA synthetase, alpha chain; Succinyl-CoA synthetase, beta chain
EC
6.2.1.4
UniProt
P53590
Ligands
SO4
Pockets
4 · best druggability 0.79

Structure

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

ChainMoleculeTypeResiduesSecondary structureUniProt
ASuccinyl-CoA synthetase, alpha chain (EC 6.2.1.4)protein30637% helix, 22% strand—
BSuccinyl-CoA synthetase, beta chain (EC 6.2.1.4)protein39538% helix, 25% strandP53590

Ligands and binding sites

  • SO4 · Sulfate ion · ion · 2 copies · chains B, A

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

Pockets

4 pockets found on a 1 Å grid, 3 with a druggability of 0.5 or more.

PocketVolume (ų)DruggabilityBuriednessLining residuesInside
110750.790.81105SO4
21600.560.8228empty
32000.510.7722SO4
4570.290.7414empty

Interfaces

1 interface between chains.

  • A–B · 2213 Ų buried · 32 hydrogen bonds · protein-protein

Modifications

Observed in the structure: 3 modified (artifact, oxidation, phosphorylation).

Compared structures

  • 1EUD · Crystal structure of phosphorylated pig heart, GTP-specific succinyl-CoA synthetase · the same entry in another collection · chain A against A, TM-score 1.00
  • P53590 · AlphaFold monomer V2.0 prediction for succinate--CoA ligase [GDP- forming] subunit beta… · a predicted model of the same protein · chain B against A, TM-score 0.89

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