› 2gux

X-ray diffraction
2Å resolution

Selenomethionine derivative of griffithsin

Released:
DOI: 10.2210/pdb2gux/pdb
PDB 2gux coloured by chain and viewed from the front.
PDB 2gux coloured by chain and viewed from the side.
PDB 2gux coloured by chain and viewed from the top.
Source organism: Griffithsia
Primary publication:
Domain-swapped structure of the potent antiviral protein griffithsin and its mode of carbohydrate binding.
Ziółkowska NE, O'Keefe BR, Mori T, Zhu C, Giomarelli B, Vojdani F, Palmer KE, McMahon JB, Wlodawer A
Structure 14 1127-35 (2006)
PMID: 16843894

Function and Biology Details

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

Structure analysis Details

Assembly composition:
homo dimer (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Griffithsin Chain: A
Molecule details ›
Chain: A
Length: 138 amino acids
Theoretical weight: 14.61 KDa
Source organism: Griffithsia
Expression system: Escherichia coli
UniProt:
  • Canonical: P84801 (Residues: 1-121; Coverage: 100%)
Sequence domains: Jacalin-like lectin domain
Structure domains: Jacalin-like lectin domain

Ligands and Environments

1 bound ligand:
Ligand SO4 1 x SO4
1 modified residue:
Ligand MSE 2 x MSE

Experiments and Validation Details

Entry percentile scores
X-ray source: APS BEAMLINE 22-ID
Spacegroup: P3221
Unit cell:
a: 66.87Å b: 66.87Å c: 68.2Å
α: 90° β: 90° γ: 120°
R-values:
R R work R free
0.189 0.189 0.254
Expression system: Escherichia coli

Quick links

Citations

19 review citations

Griffithsin, a Highly Potent Broad-Spectrum Antiviral Lectin from Red Algae: From Discovery to Clinical Application.
Lee C. (2019)
18 more