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Pea lectin-sucrose complex

Analyse Pea lectin-sucrose complex in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB
1OFS
Type
protein
Length
458 residues
Chains
4
Method
x-ray diffraction
Collection
MolNFT v1 / PDB
Contract
0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner
0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule
Pea lectin alpha chain; Pea lectin beta chain
UniProt
P02867
Ligands
GLC, FRU, MN, CA
Pockets
2 · best druggability 0.40

Structure

x-ray diffraction · 2 distinct chains · 4% helix, 48% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
A, CPea lectin alpha chainprotein1813% helix, 45% strandP02867
B, DPea lectin beta chainprotein486% helix, 63% strandP02867

Ligands and binding sites

  • GLC · alpha-D-glucopyranose · sugar · 2 copies · chains A, B, C, D
  • FRU · beta-D-fructofuranose · sugar · 2 copies · chains A, B, C, D
  • MN · Manganese (II) ion · metal · 2 copies · chains A, C
  • CA · Calcium ion · metal · 2 copies · chains A, C

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

Pockets

2 pockets found on a 1 Å grid, 0 with a druggability of 0.5 or more.

PocketVolume (ų)DruggabilityBuriednessLining residuesInside
1980.400.7721empty
2710.390.7915empty

Interfaces

5 interfaces between chains.

  • A–B · 3885 Ų buried · 98 hydrogen bonds · protein-protein
  • C–D · 3874 Ų buried · 96 hydrogen bonds · protein-protein
  • A–C · 838 Ų buried · 18 hydrogen bonds · protein-protein
  • A–D · 158 Ų buried · 1 hydrogen bond · protein-protein
  • B–C · 146 Ų buried · 1 hydrogen bond · protein-protein

Compared structures

  • 1OFS · Pea lectin-sucrose complex · the same entry in another collection · chain A against A, TM-score 1.00
  • P02867 · AlphaFold monomer V2.0 prediction for lectin (P02867) · a predicted model of the same protein · chain A against A, TM-score 0.99

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