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X-ray structure of the levansucrase from erwinia amylovora

Analyse X-ray structure of the levansucrase from erwinia amylovora in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB
4D47
Type
protein
Length
3,288 residues
Chains
8
Method
x-ray diffraction
Collection
MolNFT v1 / PDB
Contract
0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner
0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule
Levansucrase
EC
2.4.1.10
UniProt
D4IGH9
Ligands
FRU, GLC
Pockets
20 · best druggability 0.85

Structure

x-ray diffraction · 1 distinct chain · 8% helix, 48% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
A, B, C, D, E, F, G, HLevansucrase (EC 2.4.1.10)protein4118% helix, 48% strandD4IGH9

Ligands and binding sites

  • FRU · beta-D-fructofuranose · sugar · 8 copies · chains A, B, C, D, E, F, G, H
  • GLC · alpha-D-glucopyranose · sugar · 8 copies · chains A, B, C, D, E, F, G, H

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

Pockets

20 pockets found on a 1 Å grid, 19 with a druggability of 0.5 or more.

PocketVolume (ų)DruggabilityBuriednessLining residuesInside
19650.850.87144empty
28590.780.8194empty
311740.780.80105empty
4620.720.9818empty
5660.720.9719empty

Interfaces

16 interfaces between chains.

  • E–F · 1151 Ų buried · 18 hydrogen bonds · protein-protein
  • C–D · 1142 Ų buried · 18 hydrogen bonds · protein-protein
  • G–H · 1137 Ų buried · 17 hydrogen bonds · protein-protein
  • A–B · 1134 Ų buried · 17 hydrogen bonds · protein-protein
  • A–H · 796 Ų buried · 8 hydrogen bonds · protein-protein

Compared structures

  • 4D47 · X-ray structure of the levansucrase from Erwinia amylovora · the same entry in another collection · chain A against A, TM-score 1.00

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