› 1tn3

X-ray diffraction
2Å resolution

THE C-TYPE LECTIN CARBOHYDRATE RECOGNITION DOMAIN OF HUMAN TETRANECTIN

Released:
DOI: 10.2210/pdb1tn3/pdb
PDB entry 1tn3 coloured by chain, front view.
PDB entry 1tn3 coloured by chain, side view.
PDB entry 1tn3 coloured by chain, top view.
Source organism: Homo sapiens
Primary publication:
Structure of the C-type lectin carbohydrate recognition domain of human tetranectin.
Kastrup JS, Nielsen BB, Rasmussen H, Holtet TL, Graversen JH, Etzerodt M, Thøgersen HC, Larsen IK
Acta Crystallogr D Biol Crystallogr 54 757-66 (1998)
PMID: 9757090

Function and Biology Details

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

Structure analysis Details

Assembly composition:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-138673 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Tetranectin Chain: A
Molecule details ›
Chain: A
Length: 137 amino acids
Theoretical weight: 15.14 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
UniProt:
  • Canonical: P05452 (Residues: 66-202; Coverage: 76%)
Gene names: CLEC3B, TNA
Sequence domains: Lectin C-type domain
Structure domains: Mannose-Binding Protein A, subunit A

Ligands and Environments

3 bound ligands:
Ligand CA 2 x CA
Ligand SO4 1 x SO4
Ligand EOH 1 x EOH
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: EMBL/DESY, HAMBURG BEAMLINE X11
Spacegroup: P42212
Unit cell:
a: 64.25Å b: 64.25Å c: 75.8Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.218 0.215 0.26
Expression system: Escherichia coli

Quick links

Citations

5 review citations

The C-type lectin-like domain superfamily.
Zelensky et al. (2005)
4 more

13 mentions without citation

Beyond Antibodies as Binding Partners: The Role of Antibody Mimetics in Bioanalysis.
Yu et al. (2017)
12 more