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Propionibacterium shermanii transcarboxylase 5S subunit bound to oxaloacetate

Analyse Propionibacterium shermanii transcarboxylase 5S subunit bound to oxaloacetate in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB
1RQE
Type
protein
Length
472 residues
Chains
1
Method
x-ray diffraction
Collection
MolNFT v1 / PDB
Contract
0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner
0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule
Transcarboxylase 5S subunit
EC
2.1.3.1
UniProt
Q70AC7
Ligands
OAA, CO
Pockets
3 · best druggability 0.69

Structure

x-ray diffraction · 1 distinct chain · 49% helix, 10% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
ATranscarboxylase 5S subunit (EC 2.1.3.1)protein47249% helix, 10% strandQ70AC7

Ligands and binding sites

  • OAA · Oxaloacetate ion · ligand · chains A
  • CO · Cobalt (II) ion · metal · chains A

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

Pockets

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

PocketVolume (ų)DruggabilityBuriednessLining residuesInside
15600.690.7965OAA, CO
21060.460.7917empty
3580.280.7412empty

Compared structures

  • 1RQE · Propionibacterium shermanii transcarboxylase 5S subunit bound to oxaloacetate · the same entry in another collection · chain A against A, TM-score 1.00
  • Q70AC7 · AlphaFold monomer V2.0 prediction for methylmalonyl-CoA carboxyltransferase 5S subunit… · a predicted model of the same protein · chain A against A, TM-score 0.98

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