3a2a

X-ray diffraction
2Å resolution

The structure of the carboxyl-terminal domain of the human voltage-gated proton channel Hv1

Released:

Function and Biology Details

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

Structure analysis Details

Assembly composition:
homo dimer (preferred)
PDBe Complex ID:
PDB-CPX-188429 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Voltage-gated hydrogen channel 1 Chains: A, B, C, D
Molecule details ›
Chains: A, B, C, D
Length: 58 amino acids
Theoretical weight: 6.71 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
UniProt:
  • Canonical: Q96D96 (Residues: 221-273; Coverage: 19%)
Gene names: HVCN1, UNQ578/PRO1140, VSOP
Sequence domains: C-terminal membrane-localisation domain of ion-channel, VCN1
Structure domains: Single alpha-helices involved in coiled-coils or other helix-helix interfaces

Ligands and Environments

1 bound ligand:
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: PHOTON FACTORY BEAMLINE BL-17A
Spacegroup: P43
Unit cell:
a: 37.65Å b: 37.65Å c: 137.04Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.253 0.252 0.266
Expression system: Escherichia coli