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Carbohydrate recognition of C-terminal half of lactoferrin: crystal structure of the complex of C-lobe with rhamnose at 2.15 a resolution

Analyse Carbohydrate recognition of C-terminal half of lactoferrin: crystal structure… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB
2E0S
Type
protein
Length
341 residues
Chains
1
Method
x-ray diffraction
Collection
MolNFT v1 / PDB
Contract
0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner
0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule
Lactotransferrin
UniProt
P24627
Ligands
NAG, BMA, MAN, RAM, ZN, FE, CO3, SO4
Pockets
4 · best druggability 0.72

Structure

x-ray diffraction · 1 distinct chain · 33% helix, 18% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
ALactotransferrinprotein34133% helix, 18% strandP24627

Ligands and binding sites

  • NAG · 2-acetamido-2-deoxy-beta-D-glucopyranose · sugar · 6 copies · chains A
  • BMA · beta-D-mannopyranose · sugar · 4 copies · chains A
  • MAN · alpha-D-mannopyranose · sugar · 3 copies · chains A
  • RAM · alpha-L-rhamnopyranose · sugar · chains A
  • ZN · Zinc ion · metal · 2 copies · chains A
  • FE · Fe (III) ion · metal · chains A
  • CO3 · Carbonate ion · ion · chains A
  • SO4 · Sulfate ion · ion · chains A

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

Pockets

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

PocketVolume (ų)DruggabilityBuriednessLining residuesInside
12730.720.8641empty
2920.320.7329NAG
3560.290.7511empty
4580.290.7412empty

Modifications

Observed in the structure: 10 disulfide, 3 glycan (disulfide, N-glycosylation).

Compared structures

  • 2E0S · Carbohydrate recognition of C-terminal half of lactoferrin: Crystal structure of the… · the same entry in another collection · chain A against A, TM-score 1.00

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