› 5io9

X-ray diffraction
1.3Å resolution

X-RAY STRUCTURE OF THE N-TERMINAL DOMAIN OF HUMAN DOUBLECORTIN

Released:
DOI: 10.2210/pdb5io9/pdb
PDB entry 5io9 coloured by chain, front view.
PDB entry 5io9 coloured by chain, side view.
PDB entry 5io9 coloured by chain, top view.
Source organism: Homo sapiens
Primary publication:
Crystal Structures of the Human Doublecortin C- and N-terminal Domains in Complex with Specific Antibodies.
Burger D, Stihle M, Sharma A, Di Lello P, Benz J, D'Arcy B, Debulpaep M, Fry D, Huber W, Kremer T, Laeremans T, Matile H, Ross A, Rufer AC, Schoch G, Steinmetz MO, Steyaert J, Rudolph MG, Thoma R, Ruf A
J Biol Chem 291 16292-306 (2016)
PMID: 27226599

Function and Biology Details

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

Structure analysis Details

Assembly composition:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-129017 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Neuronal migration protein doublecortin Chains: A, B
Molecule details ›
Chains: A, B
Length: 106 amino acids
Theoretical weight: 12.2 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
UniProt:
  • Canonical: O43602 (Residues: 52-149; Coverage: 27%)
Gene names: DBCN, DCX, LISX
Sequence domains: Doublecortin
Structure domains: Doublecortin domain

Ligands and Environments

No bound ligands
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: SLS BEAMLINE X10SA
Spacegroup: P1
Unit cell:
a: 27.026Å b: 37.783Å c: 47.752Å
α: 88.65° β: 105.78° γ: 96.55°
R-values:
R R work R free
0.188 0.186 0.21
Expression system: Escherichia coli

Quick links

Citations

1 review citation

Structure-Guided Prediction of the Functional Impact of DCLK1 Mutations on Tumorigenesis.
Carli et al. (2023)
7 other articles

2 mentions without citation

Pseudo-repeats in doublecortin make distinct mechanistic contributions to microtubule regulation.
Manka et al. (2020)
1 more