› 5e52

X-ray diffraction
2.68Å resolution

Crystal structure of human CNTN5 FN1-FN3 domains

Released:
DOI: 10.2210/pdb5e52/pdb
Model geometry
Fit model/data
PDB entry 5e52 coloured by chain, front view.
PDB entry 5e52 coloured by chain, side view.
PDB entry 5e52 coloured by chain, top view.
Source organism: Homo sapiens
Primary publication:
Structural Basis for Interactions Between Contactin Family Members and Protein-tyrosine Phosphatase Receptor Type G in Neural Tissues.
Nikolaienko RM, Hammel M, Dubreuil V, Zalmai R, Hall DR, Mehzabeen N, Karuppan SJ, Harroch S, Stella SL, Bouyain S
J Biol Chem 291 21335-21349 (2016)
PMID: 27539848

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-131753 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Contactin-5 Chain: A
Molecule details ›
Chain: A
Length: 299 amino acids
Theoretical weight: 32.51 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: O94779 (Residues: 671-969; Coverage: 28%)
Gene name: CNTN5
Sequence domains: Fibronectin type III domain

Ligands and Environments

1 bound ligand:
Ligand PO4 1 x PO4
No modified residues

Experiments and Validation Details

wwPDB Validation report is not available for this entry.
X-ray source: APS BEAMLINE 22-ID
Spacegroup: C2221
Unit cell:
a: 83.77Å b: 154.518Å c: 90.417Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.198 0.194 0.231
Expression system: Escherichia coli BL21(DE3)

Quick links

Citations

10 review citations

Conserved and Diverse Traits of Adhesion Devices from Siphoviridae Recognizing Proteinaceous or Saccharidic Receptors.
Goulet et al. (2020)
9 more

1 mention without citation

Structural Basis for Interactions Between Contactin Family Members and Protein-tyrosine Phosphatase Receptor Type G in Neural Tissues.
Nikolaienko et al. (2016)