1sz6

X-ray diffraction
2.05Å resolution

MISTLETOE LECTIN I FROM VISCUM ALBUM. CRYSTAL STRUCTURE AT 2.05 A RESOLUTION

Released:
Source organism: Viscum album
Entry authors: Gabdoulkhakov AG, Guhlistova NE, Lyashenko AV, Krauspenhaar R, Stoeva S, Voelter W, Nikonov SV, Betzel C, Mikhailov AM

Function and Biology Details

Reaction catalysed:
Endohydrolysis of the N-glycosidic bond at one specific adenosine on the 28S rRNA.
Biochemical function:
Cellular component:
  • not assigned

Structure analysis Details

Assembly composition:
hetero tetramer (preferred)
PDBe Complex ID:
PDB-CPX-160521 (preferred)
Entry contents:
2 distinct polypeptide molecules
Macromolecules (2 distinct):
Beta-galactoside-specific lectin 1 chain A isoform 1 Chain: A
Molecule details ›
Chain: A
Length: 249 amino acids
Theoretical weight: 27.23 KDa
Source organism: Viscum album
UniProt:
  • Canonical: P81446 (Residues: 34-282; Coverage: 47%)
Sequence domains: Ribosome inactivating protein
Structure domains:
Beta-galactoside-specific lectin 1 chain B Chain: B
Molecule details ›
Chain: B
Length: 263 amino acids
Theoretical weight: 28.47 KDa
Source organism: Viscum album
UniProt:
  • Canonical: P81446 (Residues: 302-564; Coverage: 50%)
Sequence domains: Ricin-type beta-trefoil lectin domain
Structure domains: Trefoil (Acidic Fibroblast Growth Factor, subunit A)

Ligands and Environments

No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: EMBL/DESY, HAMBURG BEAMLINE BW7B
Spacegroup: P6522
Unit cell:
a: 106.88Å b: 106.88Å c: 310.74Å
α: 90° β: 90° γ: 120°
R-values:
R R work R free
0.213 0.211 0.253