› 2vuv

X-ray diffraction
1.3Å resolution

Function and Biology Details

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

Structure analysis Details

Assembly composition:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-174720 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
C-type lectin domain-containing protein Chain: A
Molecule details ›
Chain: A
Length: 129 amino acids
Theoretical weight: 14.19 KDa
Source organism: Codakia orbicularis
UniProt:
  • Canonical: Q3KVL7 (Residues: 20-148; Coverage: 100%)
Sequence domains: Lectin C-type domain
Structure domains: Mannose-Binding Protein A, subunit A

Ligands and Environments

3 bound ligands:
Ligand CA 1 x CA
Ligand GOL 2 x GOL
Ligand CIT 1 x CIT
1 modified residue:
Ligand HYP 1 x HYP

Experiments and Validation Details

Entry percentile scores
X-ray source: ESRF BEAMLINE ID14-1
Spacegroup: C2
Unit cell:
a: 82.908Å b: 30.395Å c: 67.088Å
α: 90° β: 133.86° γ: 90°
R-values:
R R work R free
0.145 0.144 0.161

Quick links

Citations

2 review citations

Binding sugars: from natural lectins to synthetic receptors and engineered neolectins.
Arnaud et al. (2013)
1 more

1 mention without citation

High affinity interaction between a bivalve C-type lectin and a biantennary complex-type N-glycan revealed by crystallography and microcalorimetry.
Gourdine et al. (2008)