› 6l93

X-ray diffraction
4.47Å resolution

X-ray structure of the ligand-free human TRPV1 ankyrin repeat domain

Released:
DOI: 10.2210/pdb6l93/pdb
PDB entry 6l93 coloured by chain, front view.
PDB entry 6l93 coloured by chain, side view.
PDB entry 6l93 coloured by chain, top view.
Source organism: Homo sapiens
Primary publication:
Structure determination of the human TRPV1 ankyrin-repeat domain under nonreducing conditions.
Tanaka M, Hayakawa K, Ogawa N, Kurokawa T, Kitanishi K, Ite K, Matsui T, Mori Y, Unno M
Acta Crystallogr F Struct Biol Commun 76 130-137 (2020)
PMID: 32133998

Function and Biology Details

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

Structure analysis Details

Assembly composition:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-185513 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Transient receptor potential cation channel subfamily V member 1 Chains: A, B, C, D, E, F
Molecule details ›
Chains: A, B, C, D, E, F
Length: 280 amino acids
Theoretical weight: 30.83 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
UniProt:
  • Canonical: Q8NER1 (Residues: 101-365; Coverage: 32%)
Gene names: TRPV1, VR1
Sequence domains:

Ligands and Environments

No bound ligands
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: PHOTON FACTORY BEAMLINE BL-17A
Spacegroup: C2
Unit cell:
a: 184.228Å b: 167.414Å c: 112.632Å
α: 90° β: 108.375° γ: 90°
R-values:
R R work R free
0.223 0.22 0.27
Expression system: Escherichia coli

Quick links

Citations

1 review citation

The interaction of TRPV1 and lipids: Insights into lipid metabolism.
Abdalla et al. (2022)
1 other article

4 mentions without citation

A review of non-prostanoid, eicosanoid receptors: expression, characterization, regulation, and mechanism of action.
Biringer RG. (2022)
3 more