› 6e7y

Electron Microscopy
3.57Å resolution

cryo-EM structure of human TRPML1 with PI45P2

Released:
DOI: 10.2210/pdb6e7y/pdb
PDB entry 6e7y coloured by chain, front view.
PDB entry 6e7y coloured by chain, side view.
PDB entry 6e7y coloured by chain, top view.
Source organism: Homo sapiens
Primary publication:
Structural basis for PtdInsP2-mediated human TRPML1 regulation.
Fine M, Schmiege P, Li X
OpenAccess logo Nat Commun 9 4192 (2018)
PMID: 30305615
Related structures: EMD-9001

Function and Biology Details

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

Structure analysis Details

Assembly composition:
homo tetramer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-190453 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Mucolipin-1 Chains: A, B, C, D
Molecule details ›
Chains: A, B, C, D
Length: 580 amino acids
Theoretical weight: 65.08 KDa
Source organism: Homo sapiens
Expression system: Homo sapiens
UniProt:
  • Canonical: Q9GZU1 (Residues: 1-580; Coverage: 100%)
Gene names: MCOLN1, ML4, MSTP080, TRPML1
Sequence domains:

Ligands and Environments

1 bound ligand:
Ligand PIO 4 x PIO
No modified residues

Experiments and Validation Details

wwPDB Validation report is not available for this EM entry.
Resolution: 3.57Å
Relevant EMDB volumes: EMD-9001
Expression system: Homo sapiens

Quick links

Citations

20 review citations

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

1 mention without citation

Targeting TRP channels: recent advances in structure, ligand binding, and molecular mechanisms.
Huang et al. (2023)