› 2c6u

X-ray diffraction
1.6Å resolution

Crystal structure of human CLEC-2 (CLEC1B)

Released:
DOI: 10.2210/pdb2c6u/pdb
PDB entry 2c6u coloured by chain, front view.
PDB entry 2c6u coloured by chain, side view.
PDB entry 2c6u coloured by chain, top view.
Source organism: Homo sapiens
Primary publication:
The crystal structure and mutational binding analysis of the extracellular domain of the platelet-activating receptor CLEC-2.
Watson AA, Brown J, Harlos K, Eble JA, Walter TS, O'Callaghan CA
J Biol Chem 282 3165-72 (2007)
PMID: 17132623

Function and Biology Details

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

Structure analysis Details

Assembly composition:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-192813 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
C-type lectin domain family 1 member B Chain: A
Molecule details ›
Chain: A
Length: 122 amino acids
Theoretical weight: 14.6 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: Q9P126 (Residues: 100-221; Coverage: 53%)
Gene names: CLEC1B, CLEC2, UNQ721/PRO1384
Sequence domains: Lectin C-type domain
Structure domains: Mannose-Binding Protein A, subunit A

Ligands and Environments

No bound ligands
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: SRS BEAMLINE PX14.1
Spacegroup: P212121
Unit cell:
a: 35.064Å b: 55.065Å c: 56.165Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.161 0.159 0.198
Expression system: Escherichia coli BL21(DE3)

Quick links

Citations

19 review citations

Platelets and cancer: a casual or causal relationship: revisited.
Menter et al. (2014)
18 more

8 mentions without citation

Fucoidan's Molecular Targets: A Comprehensive Review of Its Unique and Multiple Targets Accounting for Promising Bioactivities Supported by In Silico Studies.
Zayed et al. (2023)
7 more