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Structure of putative oorc subunit of 2-OXOGLUTARATE:ACCEPTOR oxidoreductase from campylobacter jejuni

Analyse Structure of putative oorc subunit of 2-OXOGLUTARATE:ACCEPTOR oxidoreductase… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB
3G2E
Type
protein
Length
735 residues
Chains
4
Method
x-ray diffraction
Collection
MolNFT v1 / PDB
Contract
0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner
0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule
Oorc subunit of 2-OXOGLUTARATE:ACCEPTOR oxidoreductase
UniProt
Q0PAX8
Pockets
7 · best druggability 0.84

Structure

x-ray diffraction · 3 distinct chains · 45% helix, 24% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
AOorc subunit of 2-OXOGLUTARATE:ACCEPTOR oxidoreductaseprotein18446% helix, 23% strandQ0PAX8
B, DOorc subunit of 2-OXOGLUTARATE:ACCEPTOR oxidoreductaseprotein18544% helix, 23% strandQ0PAX8
COorc subunit of 2-OXOGLUTARATE:ACCEPTOR oxidoreductaseprotein18146% helix, 24% strandQ0PAX8

Ligands and binding sites

  • GOL · Glycerol · additive · chains C

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

Pockets

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

PocketVolume (ų)DruggabilityBuriednessLining residuesInside
110400.840.8595empty
28760.780.8180empty
33180.520.7434empty
41250.490.8019empty
5930.340.7422empty

Interfaces

6 interfaces between chains.

  • A–B · 2767 Ų buried · 62 hydrogen bonds · protein-protein
  • A–C · 1267 Ų buried · 18 hydrogen bonds · protein-protein
  • B–D · 1245 Ų buried · 20 hydrogen bonds · protein-protein
  • C–D · 523 Ų buried · 8 hydrogen bonds · protein-protein
  • B–C · 215 Ų buried · 0 hydrogen bonds · protein-protein

Compared structures

  • 3G2E · Structure of putative OORC subunit of 2-oxoglutarate:acceptor oxidoreductase from… · the same entry in another collection · chain A against A, TM-score 1.00

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