› 6flk

X-ray diffraction
1.6Å resolution

Crystal structure of Cep120 C2C domain

Released:
DOI: 10.2210/pdb6flk/pdb
PDB entry 6flk coloured by chain, front view.
PDB entry 6flk coloured by chain, side view.
PDB entry 6flk coloured by chain, top view.
Source organism: Homo sapiens
Primary publication:
Cep120 promotes microtubule formation through a unique tubulin binding C2 domain.
Sharma A, Gerard SF, Olieric N, Steinmetz MO
J Struct Biol 203 62-70 (2018)
PMID: 29398280

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-185444 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Centrosomal protein of 120 kDa Chains: A, B
Molecule details ›
Chains: A, B
Length: 163 amino acids
Theoretical weight: 18.54 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
UniProt:
  • Canonical: Q8N960 (Residues: 450-610; Coverage: 16%)
Gene names: CCDC100, CEP120
Sequence domains: C2 domain

Ligands and Environments

No bound ligands
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: SLS BEAMLINE X06DA
Spacegroup: P1
Unit cell:
a: 32.4Å b: 40.954Å c: 69.132Å
α: 102.47° β: 98.07° γ: 89.92°
R-values:
R R work R free
0.2 0.197 0.246
Expression system: Escherichia coli

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Citations

5 citation in other articles

A novel Cep120-dependent mechanism inhibits centriole maturation in quiescent cells.
Betleja et al. (2018)
4 more