› 6fnz

X-ray diffraction
2.23Å resolution

Crystal Structure of domain-swapped C-terminal domain of human doublecortin

Released:
DOI: 10.2210/pdb6fnz/pdb
PDB entry 6fnz coloured by chain, front view.
PDB entry 6fnz coloured by chain, side view.
PDB entry 6fnz coloured by chain, top view.
Source organisms:
Primary publication:
Domain swap in the C-terminal ubiquitin-like domain of human doublecortin.
Rufer AC, Kusznir E, Burger D, Stihle M, Ruf A, Rudolph MG
Acta Crystallogr D Struct Biol 74 450-462 (2018)
PMID: 29717716

Function and Biology Details

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

Structure analysis Details

Assemblies composition:
hetero trimer (preferred)
hetero tetramer
Assembly name:
PDBe Complex ID:
PDB-CPX-129022 (preferred)
Entry contents:
2 distinct polypeptide molecules
Macromolecules (2 distinct):
Neuronal migration protein doublecortin Chains: A, B, C, D
Molecule details ›
Chains: A, B, C, D
Length: 81 amino acids
Theoretical weight: 9.09 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: O43602 (Residues: 174-254; Coverage: 22%)
Gene names: DBCN, DCX, LISX
Sequence domains: Doublecortin
possible peptide Chains: E, F, G
Molecule details ›
Chains: E, F, G
Length: 6 amino acids
Theoretical weight: 605 Da
Source organism: unidentified
Expression system: Escherichia coli BL21(DE3)

Ligands and Environments

No bound ligands
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: SLS BEAMLINE X10SA
Spacegroup: P43212
Unit cell:
a: 98.45Å b: 98.45Å c: 114.81Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.209 0.208 0.231
Expression system: Escherichia coli BL21(DE3)

Quick links

Citations

1 review citation

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

1 mention without citation

Doublecortin engages the microtubule lattice through a cooperative binding mode involving its C-terminal domain.
Rafiei et al. (2022)