MolNFT v1 · #57266 · protein
The structure of the carboxyl-terminal domain of the human voltage- gated proton channel HV1
3A2A: “The structure of the carboxyl-terminal domain of the human voltage- gated proton channel HV1”. X-ray diffraction. MolNFT v1 #57266 on GenesisL1: 3D structure, binding sites and pockets in GL1X.
- PDB
- 3A2A
- Type
- protein
- Length
- 164 residues
- Chains
- 4
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- UniProt
- Q96D96
Structure
x-ray diffraction · 1 distinct chain.
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, B, C, D | — | protein | 41 | — | Q96D96 |
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
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