› 4q56

X-ray diffraction
1.38Å resolution

Structure of Helix aspersa agglutinin with natural glycosylation and N-acetyl-alpha-D-galactosamine (GalNAc)

Released:
DOI: 10.2210/pdb4q56/pdb
PDB 4q56 coloured by chain and viewed from the front.
PDB 4q56 coloured by chain and viewed from the side.
PDB 4q56 coloured by chain and viewed from the top.
Source organism: Helix aspersa
Primary publication:
Structural studies of Helix aspersa agglutinin complexed with GalNAc: A lectin that serves as a diagnostic tool.
Pietrzyk AJ, Bujacz A, Mak P, Potempa B, Niedziela T
Int. J. Biol. Macromol. (2015)
PMID: 26416237

Function and Biology Details

Biochemical function:
Biological process:
Cellular component:
  • not assigned
Sequence domains:

Structure analysis Details

Assembly composition:
homo hexamer (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecules (2 distinct):
H_lectin domain-containing protein Chain: A
Molecule details ›
Chain: A
Length: 101 amino acids
Theoretical weight: 11.35 KDa
Source organism: Helix aspersa
UniProt:
  • Canonical: A0A0R4I963 (Residues: 1-101; Coverage: 100%)
Sequence domains: H-type lectin domain
Structure domains: Immunoglobulin-like

Ligands and Environments

Carbohydrate polymer : NEW Components: NAG, FUC, GAL, BMA
Ligand NAG 2 x NAG
Ligand FUC 2 x FUC
Ligand GAL 1 x GAL
Ligand BMA 1 x BMA
4 bound ligands:
Ligand ACT 1 x ACT
Ligand A2G 1 x A2G
Ligand NA 1 x NA
Ligand ZN 1 x ZN
1 modified residue:
Ligand PCA 1 x PCA

Experiments and Validation Details

Entry percentile scores
X-ray source: PETRA III, EMBL c/o DESY BEAMLINE P13 (MX1)
Spacegroup: R32
Unit cell:
a: 47.9Å b: 47.9Å c: 281.53Å
α: 90° β: 90° γ: 120°
R-values:
R R work R free
0.138 0.137 0.168

Quick links

Citations

1 citations in other articles

The purplish bifurcate mussel Mytilisepta virgata gene expression atlas reveals a remarkable tissue functional specialization.
Gerdol et al. (2017)