› 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 entry 4q56 coloured by chain, front view.
PDB entry 4q56 coloured by chain, side view.
PDB entry 4q56 coloured by chain, top view.
Source organism: Cornu aspersum
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 81 1059-68 (2015)
PMID: 26416237

Function and Biology Details

Biochemical function:
Biological process:
Cellular component:
Sequence domains:

Structure analysis Details

Assembly composition:
homo hexamer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-102623 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecules (2 distinct):
H-type lectin domain-containing protein Chain: A
Molecule details ›
Chain: A
Length: 101 amino acids
Theoretical weight: 11.35 KDa
Source organism: Cornu aspersum
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
Carbohydrate polymer
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

2 review citations

Mollusc N-glycosylation: Structures, Functions and Perspectives.
Staudacher E. (2021)
1 more