› 3wbr

X-ray diffraction
2.2Å resolution

Crystal structure of carbohydrate recognition domain of Blood Dendritic Cell Antigen-2 (BDCA2) lectin (crystal form-3)

Released:
DOI: 10.2210/pdb3wbr/pdb
PDB entry 3wbr coloured by chain, front view.
PDB entry 3wbr coloured by chain, side view.
PDB entry 3wbr coloured by chain, top view.
Source organism: Homo sapiens
Primary publication:
Crystal structures of carbohydrate recognition domain of blood dendritic cell antigen-2 (BDCA2) reveal a common domain-swapped dimer.
Nagae M, Ikeda A, Kitago Y, Matsumoto N, Yamamoto K, Yamaguchi Y
Proteins 82 1512-8 (2014)
PMID: 24425442

Function and Biology Details

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

Structure analysis Details

Assembly composition:
homo dimer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-186703 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
C-type lectin domain family 4 member C Chains: A, B, C, D, E, F, G, H
Molecule details ›
Chains: A, B, C, D, E, F, G, H
Length: 130 amino acids
Theoretical weight: 15.13 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
UniProt:
  • Canonical: Q8WTT0 (Residues: 83-210; Coverage: 60%)
Gene names: BDCA2, CLEC4C, CLECSF11, CLECSF7, DLEC, HECL, UNQ9361/PRO34150
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: PHOTON FACTORY BEAMLINE BL-17A
Spacegroup: P43212
Unit cell:
a: 86.13Å b: 86.13Å c: 431.71Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.255 0.253 0.295
Expression system: Escherichia coli

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Citations

2 review citations

What contributes to an effective mannose recognition domain?
Sager et al. (2017)
1 more