› 2nu5

X-ray diffraction
1.56Å resolution

Crystal structure of a complex of griffithsin cocrystallized with N-acetylglucosamine

Released:
DOI: 10.2210/pdb2nu5/pdb
PDB entry 2nu5 coloured by chain, front view.
PDB entry 2nu5 coloured by chain, side view.
PDB entry 2nu5 coloured by chain, top view.
Source organism: Griffithsia sp. Q66D336
Primary publication:
Crystallographic studies of the complexes of antiviral protein griffithsin with glucose and N-acetylglucosamine.
Ziółkowska NE, Shenoy SR, O'Keefe BR, Wlodawer A
Protein Sci 16 1485-9 (2007)
PMID: 17567736

Function and Biology Details

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

Structure analysis Details

Assembly composition:
homo dimer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-160913 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Griffithsin Chains: A, B
Molecule details ›
Chains: A, B
Length: 122 amino acids
Theoretical weight: 12.73 KDa
Source organism: Griffithsia sp. Q66D336
Expression system: Nicotiana benthamiana
UniProt:
  • Canonical: P84801 (Residues: 1-121; Coverage: 100%)
Sequence domains: Jacalin-like lectin domain
Structure domains: Jacalin-like lectin domain

Ligands and Environments

2 bound ligands:
Ligand NAG 6 x NAG
Ligand SO4 3 x SO4
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: APS BEAMLINE 22-ID
Spacegroup: P212121
Unit cell:
a: 37.57Å b: 53.41Å c: 104.01Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.165 0.163 0.205
Expression system: Nicotiana benthamiana

Quick links

Citations

5 review citations

Griffithsin: An Antiviral Lectin with Outstanding Therapeutic Potential.
Lusvarghi et al. (2016)
4 more

4 mentions without citation

Mannose-Specific Lectins from Marine Algae: Diverse Structural Scaffolds Associated to Common Virucidal and Anti-Cancer Properties.
Barre et al. (2019)
3 more