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Cryo-EM structure of GH31 alpha-1,3-glucosidase from lactococcus lactis subsp. cremoris

Analyse Cryo-EM structure of GH31 alpha-1,3-glucosidase from lactococcus lactis subsp.… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB
7WLG
Type
protein
Length
4,368 residues
Chains
6
Method
electron microscopy
Collection
MolNFT v1 / PDB
Contract
0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner
0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule
Alpha-xylosidase
EC
3.2.1.-
UniProt
A2RM80
Pockets
20 · best druggability 0.78

Structure

electron microscopy · 1 distinct chain · 27% helix, 23% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
A, B, C, D, E, FAlpha-xylosidase (EC 3.2.1.-)protein72827% helix, 23% strandA2RM80

Pockets

20 pockets found on a 1 Å grid, 20 with a druggability of 0.5 or more.

PocketVolume (ų)DruggabilityBuriednessLining residuesInside
110170.780.8099empty
29810.770.80100empty
39680.770.8091empty
48360.770.8054empty
58870.770.8088empty

Interfaces

12 interfaces between chains.

  • B–F · 1334 Ų buried · 10 hydrogen bonds · protein-protein
  • C–E · 1334 Ų buried · 7 hydrogen bonds · protein-protein
  • A–D · 1333 Ų buried · 6 hydrogen bonds · protein-protein
  • C–F · 835 Ų buried · 7 hydrogen bonds · protein-protein
  • B–D · 831 Ų buried · 7 hydrogen bonds · protein-protein

Compared structures

  • 7WLG · Cryo-EM structure of GH31 alpha-1,3-glucosidase from Lactococcus lactis subsp. cremoris · the same entry in another collection · chain B against B, TM-score 1.00

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