› 1dlp

X-ray diffraction
3.3Å resolution

STRUCTURAL CHARACTERIZATION OF THE NATIVE FETUIN-BINDING PROTEIN SCILLA CAMPANULATA AGGLUTININ (SCAFET): A NOVEL TWO-DOMAIN LECTIN

Released:
DOI: 10.2210/pdb1dlp/pdb
PDB entry 1dlp coloured by chain, front view.
PDB entry 1dlp coloured by chain, side view.
PDB entry 1dlp coloured by chain, top view.
Source organism: Hyacinthoides hispanica
Primary publication:
Structural characterisation of the native fetuin-binding protein Scilla campanulata agglutinin: a novel two-domain lectin.
Wright LM, Reynolds CD, Rizkallah PJ, Allen AK, Van Damme EJ, Donovan MJ, Peumans WJ
FEBS Lett 468 19-22 (2000)
PMID: 10683433

Function and Biology Details

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

Structure analysis Details

Assembly composition:
homo hexamer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-195693 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Bulb-type lectin domain-containing protein Chains: A, B, C, D, E, F
Molecule details ›
Chains: A, B, C, D, E, F
Length: 236 amino acids
Theoretical weight: 25.55 KDa
Source organism: Hyacinthoides hispanica
UniProt:
  • Canonical: Q9ZP48 (Residues: 22-257; Coverage: 89%)
Structure domains: Bulb-type lectin domain

Ligands and Environments

No bound ligands
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: SRS BEAMLINE PX9.5
Spacegroup: C2
Unit cell:
a: 277.94Å b: 164.1Å c: 53.6Å
α: 90° β: 95.38° γ: 90°
R-values:
R R work R free
0.189 0.189 0.293

Quick links

Citations

2 review citations

Lectins as bioactive plant proteins: a potential in cancer treatment.
De Mejía et al. (2005)
1 more

6 mentions without citation

Lectin-Like Bacteriocins.
Ghequire et al. (2018)
5 more