› 2gme

X-ray diffraction
1.75Å resolution

Metal-free (apo) P. angolensis seed lectin

Released:
DOI: 10.2210/pdb2gme/pdb
PDB entry 2gme coloured by chain, front view.
PDB entry 2gme coloured by chain, side view.
PDB entry 2gme coloured by chain, top view.
Source organism: Pterocarpus angolensis
Primary publication:
Interplay between metal binding and cis/trans isomerization in legume lectins: structural and thermodynamic study of P. angolensis lectin.
Garcia-Pino A, Buts L, Wyns L, Loris R
J Mol Biol 361 153-67 (2006)
PMID: 16824540

Function and Biology Details

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

Structure analysis Details

Assembly composition:
homo dimer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-184567 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Legume lectin domain-containing protein Chains: A, B
Molecule details ›
Chains: A, B
Length: 252 amino acids
Theoretical weight: 27.56 KDa
Source organism: Pterocarpus angolensis
UniProt:
  • Canonical: Q8GSD2 (Residues: 9-260; Coverage: 97%)
Sequence domains: Legume lectin domain
Structure domains: Jelly Rolls

Ligands and Environments

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

Experiments and Validation Details

Entry percentile scores
X-ray source: EMBL/DESY, HAMBURG BEAMLINE X11
Spacegroup: P212121
Unit cell:
a: 58.883Å b: 62Å c: 130.145Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.195 0.193 0.221

Quick links

Citations

1 review citation

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

1 mention without citation

'Hot' macromolecular crystals.
Koclega et al. (2009)