The structure of the carboxyl-terminal domain of the human voltage- gated proton channel HV1

Structure

x-ray diffraction · 1 distinct chain · 95% helix, 0% strand (DSSP).

Ligands and binding sites

• CL · Chloride ion · ion · 2 copies · chains A, C

Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.

Interfaces

4 interfaces between chains.

• C–D · 1112 Ų buried · 4 hydrogen bonds · protein-protein
• A–B · 1109 Ų buried · 3 hydrogen bonds · protein-protein
• A–D · 582 Ų buried · 3 hydrogen bonds · protein-protein
• B–D · 181 Ų buried · 5 hydrogen bonds · protein-protein

Modifications

Observed in the structure: 2 disulfide (disulfide).

Compared structures

• 3A2A · The structure of the carboxyl-terminal domain of the human voltage-gated proton channel… · the same entry in another collection · chain A against A, TM-score 1.00
• Q96D96 · AlphaFold monomer V2.0 prediction for voltage-gated hydrogen channel 1 (Q96D96) · a predicted model of the same protein · chain A against A, TM-score 0.94

Analyse

• Open in the research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides and crosslinks on the 3D structure
• Every structure of UniProt Q96D96
• Elsewhere: RCSB PDB 3A2A · PDBe 3A2A · UniProt Q96D96