› 6nq0

Electron Microscopy
3.7Å resolution

Cryo-EM structure of human TPC2 channel in the ligand-bound open state

Released:
DOI: 10.2210/pdb6nq0/pdb
PDB entry 6nq0 coloured by chain, front view.
PDB entry 6nq0 coloured by chain, side view.
PDB entry 6nq0 coloured by chain, top view.
Source organism: Homo sapiens
Primary publication:
Structural mechanisms of phospholipid activation of the human TPC2 channel.
She J, Zeng W, Guo J, Chen Q, Bai XC, Jiang Y
Elife 8 (2019)
PMID: 30860481
Related structures: EMD-0477

Function and Biology Details

Biochemical function:
Biological process:
Cellular component:
Sequence domains:

Structure analysis Details

Assembly composition:
homo dimer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-185559 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Two pore channel protein 2 Chains: A, B
Molecule details ›
Chains: A, B
Length: 756 amino acids
Theoretical weight: 85.67 KDa
Source organism: Homo sapiens
Expression system: Homo sapiens
UniProt:
  • Canonical: Q8NHX9 (Residues: 1-752; Coverage: 100%)
Gene names: TPC2, TPCN2
Sequence domains: Ion transport protein

Ligands and Environments

1 bound ligand:
Ligand EUJ 2 x EUJ
No modified residues

Experiments and Validation Details

Entry percentile scores
Resolution: 3.7Å
Relevant EMDB volumes: EMD-0477
Expression system: Homo sapiens

Quick links

Citations

22 review citations

Novel roles of phosphoinositides in signaling, lipid transport, and disease.
Hammond et al. (2020)
21 more

13 mentions without citation

COVID-19: Drug Targets and Potential Treatments.
Gil et al. (2020)
12 more