› 4pik

X-ray diffraction
1.7Å resolution

Function and Biology Details

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

Structure analysis Details

Assembly composition:
homo dimer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-127631 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecules (2 distinct):
Jacalin-type lectin domain-containing protein Chains: A, B, C, D
Molecule details ›
Chains: A, B, C, D
Length: 149 amino acids
Theoretical weight: 15.65 KDa
Source organism: Musa acuminata
Expression system: Escherichia coli
UniProt:
  • Canonical: O22321 (Residues: 1-141; Coverage: 100%)
Sequence domains: Jacalin-like lectin domain
Structure domains: Jacalin-like lectin domain

Ligands and Environments

Carbohydrate polymer : NEW Components: MAN
Carbohydrate polymer
2 bound ligands:
Ligand MAN 5 x MAN
Ligand GOL 4 x GOL
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: APS BEAMLINE 21-ID-D
Spacegroup: P21
Unit cell:
a: 50.456Å b: 94.708Å c: 63.347Å
α: 90° β: 97.5° γ: 90°
R-values:
R R work R free
0.165 0.163 0.187
Expression system: Escherichia coli

Quick links

Citations

19 review citations

Antiviral lectins: Selective inhibitors of viral entry.
Mitchell et al. (2017)
18 more

4 mentions without citation

Overview of the Structure⁻Function Relationships of Mannose-Specific Lectins from Plants, Algae and Fungi.
Barre et al. (2019)
3 more