› 3zee

Electron Microscopy
6.1Å resolution

Electron cyro-microscopy helical reconstruction of Par-3 N terminal domain

Released:
DOI: 10.2210/pdb3zee/pdb
PDB entry 3zee coloured by chain, front view.
PDB entry 3zee coloured by chain, side view.
PDB entry 3zee coloured by chain, top view.
Source organism: Rattus norvegicus
Primary publication:
Structural insights into the intrinsic self-assembly of Par-3 N-terminal domain.
Zhang Y, Wang W, Chen J, Zhang K, Gao F, Gao B, Zhang S, Dong M, Besenbacher F, Gong W, Zhang M, Sun F, Feng W
Structure 21 997-1006 (2013)
PMID: 23643951
Related structures: EMD-2237

Function and Biology Details

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

Structure analysis Details

Assembly composition:
homo 49-mer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-195566 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Partitioning defective 3 homolog Chain: A
Molecule details ›
Chain: A
Length: 84 amino acids
Theoretical weight: 9.55 KDa
Source organism: Rattus norvegicus
Expression system: Escherichia coli BL21
UniProt:
  • Canonical: Q9Z340 (Residues: 2-82; Coverage: 6%)
Gene names: Par3, Pard3
Sequence domains: N-terminal of Par3 and HAL proteins

Ligands and Environments

No bound ligands
No modified residues

Experiments and Validation Details

Entry percentile scores
Resolution: 6.1Å
Relevant EMDB volumes: EMD-2237
Expression system: Escherichia coli BL21

Quick links

Citations

8 review citations

The PAR proteins: from molecular circuits to dynamic self-stabilizing cell polarity.
Lang et al. (2017)
7 more

3 mentions without citation

Protein clustering for cell polarity: Par-3 as a paradigm.
Harris TJC. (2017)
2 more