MolNFT v1 · #137308 · protein

Crystal structure of human CD22 ig domains 1-3

5VKJ · B-cell receptor CD22: “Crystal structure of human CD22 ig domains 1-3”. X-ray diffraction, 3 ligands (NAG, MAN, BMA). MolNFT v1 #137308 on GenesisL1: 3D structure, binding sites and pockets in GL1X.

PDB: 5VKJ
Type: protein
Length: 312 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

Structure

x-ray diffraction · 1 distinct chain · 5% helix, 54% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	B-cell receptor CD22	protein	312	5% helix, 54% strand	P20273

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
GOL · Glycerol · additive · 4 copies · 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

5VKJ · Crystal structure of human CD22 Ig domains 1-3 · 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 0.89

Analyse

Open in the research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides and crosslinks on the 3D structure
Every structure of UniProt P20273
Elsewhere: RCSB PDB 5VKJ · PDBe 5VKJ · UniProt P20273

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