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Crystal structure of human CD22 ig domains 1-3 in complex with alpha 2-6 sialyllactose

Analyse Crystal structure of human CD22 ig domains 1-3 in complex with alpha 2-6… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB
5VKM
Type
protein
Length
306 residues
Chains
1
Method
x-ray diffraction
Collection
MolNFT v1 / PDB
Contract
0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner
0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule
B-cell receptor CD22
UniProt
P20273
Ligands
NAG, MAN, BMA, GAL, SIA

Structure

x-ray diffraction · 1 distinct chain · 3% helix, 57% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
AB-cell receptor CD22protein3063% helix, 57% strandP20273

Ligands and binding sites

  • NAG · 2-acetamido-2-deoxy-beta-D-glucopyranose · sugar · 2 copies · chains A
  • MAN · alpha-D-mannopyranose · sugar · 2 copies · chains A
  • BMA · beta-D-mannopyranose · sugar · chains A
  • GAL · beta-D-galactopyranose · sugar · chains A
  • SIA · N-acetyl-alpha-neuraminic acid · sugar · chains A
  • GOL · Glycerol · additive · chains A

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

Modifications

Observed in the structure: 4 disulfide, 1 glycan (disulfide, N-glycosylation).

Compared structures

  • 5VKM · Crystal structure of human CD22 Ig domains 1-3 in complex with alpha 2-6 sialyllactose · the same entry in another collection · chain A against A, TM-score 1.00
  • P20273 · AlphaFold monomer V2.0 prediction for B-cell receptor CD22 (P20273) · a predicted model of the same protein · chain A against A, TM-score 0.93

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