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Disproportionating enzyme 1 from arabidopsis - maltotriose soak

Analyse Disproportionating enzyme 1 from arabidopsis - maltotriose soak in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB
5CPS
Type
protein
Length
1,029 residues
Chains
2
Method
x-ray diffraction
Collection
MolNFT v1 / PDB
Contract
0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner
0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule
4-alpha-glucanotransferase DPE1, CHLOROPLASTIC/AMYLOPLASTIC
EC
2.4.1.25
UniProt
Q9LV91
Ligands
GLC
Pockets
11 · best druggability 0.76

Structure

x-ray diffraction · 2 distinct chains · 47% helix, 12% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
A4-alpha-glucanotransferase DPE1, CHLOROPLASTIC/AMYLOPLASTIC (EC 2.4.1.25)protein51747% helix, 12% strandQ9LV91
B4-alpha-glucanotransferase DPE1, CHLOROPLASTIC/AMYLOPLASTIC (EC 2.4.1.25)protein51247% helix, 12% strandQ9LV91

Ligands and binding sites

  • GLC · alpha-D-glucopyranose · sugar · 17 copies · chains A, B
  • EDO · 1,2-ethanediol · additive · 16 copies · chains A, B

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

Pockets

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

PocketVolume (ų)DruggabilityBuriednessLining residuesInside
12950.760.8832empty
26280.750.8171GLC, EDO
37410.720.7883GLC, EDO
43370.630.7931EDO
53570.600.7728EDO

Interfaces

1 interface between chains.

  • A–B · 2044 Ų buried · 25 hydrogen bonds · protein-protein

Compared structures

  • Q9LV91 · AlphaFold monomer V2.0 prediction for 4-alpha-glucanotransferase DPE1… · a predicted model of the same protein · chain B against A, TM-score 1.00

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