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The crystal structure of apo- udp-glucose pyrophosphorylase

Analyse The crystal structure of apo- udp-glucose pyrophosphorylase in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB
3JUJ
Type
protein
Length
1,092 residues
Chains
4
Method
x-ray diffraction
Collection
MolNFT v1 / PDB
Contract
0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner
0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule
Udp-glucose pyrophosphorylase (galu)
EC
2.7.7.9
UniProt
O25363
Pockets
16 · best druggability 0.90

Structure

x-ray diffraction · 1 distinct chain · 37% helix, 25% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
A, B, C, DUdp-glucose pyrophosphorylase (galu) (EC 2.7.7.9)protein27337% helix, 25% strandO25363

Pockets

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

PocketVolume (ų)DruggabilityBuriednessLining residuesInside
111090.900.92108empty
25870.730.8151empty
36430.710.7843empty
45970.700.7950empty
56540.700.7852empty

Interfaces

6 interfaces between chains.

  • A–B · 1941 Ų buried · 22 hydrogen bonds · protein-protein
  • C–D · 1912 Ų buried · 14 hydrogen bonds · protein-protein
  • A–D · 753 Ų buried · 19 hydrogen bonds · protein-protein
  • B–C · 736 Ų buried · 13 hydrogen bonds · protein-protein
  • B–D · 205 Ų buried · 0 hydrogen bonds · protein-protein

Compared structures

  • 3JUJ · The crystal structure of apo- UDP-glucose pyrophosphorylase · the same entry in another collection · chain A against A, TM-score 1.00

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