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Structure of invertase from schwanniomyces occidentalis

Analyse Structure of invertase from schwanniomyces occidentalis in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB
3KF5
Type
protein
Length
1,020 residues
Chains
2
Method
x-ray diffraction
Collection
MolNFT v1 / PDB
Contract
0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner
0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule
Invertase
EC
3.2.1.26
Ligands
NAG
Pockets
14 · best druggability 0.84

Structure

x-ray diffraction · 2 distinct chains · 1% helix, 48% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
AInvertase (EC 3.2.1.26)protein5121% helix, 48% strand—
BInvertase (EC 3.2.1.26)protein5081% helix, 47% strand—

Ligands and binding sites

  • NAG · 2-acetamido-2-deoxy-beta-D-glucopyranose · sugar · 8 copies · chains A, B
  • GOL · Glycerol · additive · 3 copies · chains A

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

Pockets

14 pockets found on a 1 Å grid, 6 with a druggability of 0.5 or more.

PocketVolume (ų)DruggabilityBuriednessLining residuesInside
12410.840.9732empty
22490.830.9537empty
33730.580.7639empty
43610.570.7636GOL
52390.550.7728empty

Interfaces

1 interface between chains.

  • A–B · 2099 Ų buried · 32 hydrogen bonds · protein-protein

Modifications

Observed in the structure: 8 glycan (N-glycosylation).

Compared structures

  • 3KF5 · Structure of invertase from Schwanniomyces occidentalis · the same entry in another collection · chain A against A, TM-score 1.00

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