MolNFT v1 · #82433 · protein
Crystal structure of a parallel coiled-coil dimerization domain from the voltage-gated proton channel (OXIDATION/H2O2)
3VMZ · Voltage-gated hydrogen channel 1: “Crystal structure of a parallel coiled-coil dimerization domain from the voltage-gated proton channel…”. X-ray diffraction, 1 pocket (best druggability 0.63). MolNFT v1 #82433 on GenesisL1: 3D…
- PDB
- 3VMZ
- Type
- protein
- Length
- 191 residues
- Chains
- 4
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Voltage-gated hydrogen channel 1
- UniProt
- Q3U2S8
- Pockets
- 1 · best druggability 0.63
Structure
x-ray diffraction · 2 distinct chains · 88% helix, 0% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, C, B | Voltage-gated hydrogen channel 1 | protein | 48 | 88% helix, 0% strand | Q3U2S8 |
| D | Voltage-gated hydrogen channel 1 | protein | 47 | 89% helix, 0% strand | Q3U2S8 |
Pockets
1 pocket found on a 1 Å grid, 1 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 366 | 0.63 | 0.79 | 33 | empty |
Interfaces
6 interfaces between chains.
- A–B · 1206 Ų buried · 5 hydrogen bonds · protein-protein
- C–D · 1193 Ų buried · 4 hydrogen bonds · protein-protein
- A–D · 287 Ų buried · 3 hydrogen bonds · protein-protein
- C–B · 31 Ų buried · 0 hydrogen bonds · protein-protein
- B–D · 21 Ų buried · 0 hydrogen bonds · protein-protein
Compared structures
- 3VMZ · Crystal Structure of a parallel coiled-coil dimerization domain from the voltage-gated… · the same entry in another collection · chain A against A, TM-score 1.00
- Q3U2S8 · AlphaFold monomer V2.0 prediction for voltage-gated hydrogen channel 1 (Q3U2S8) · a predicted model of the same protein · chain A against A, TM-score 0.96
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 Q3U2S8
- Elsewhere: RCSB PDB 3VMZ · PDBe 3VMZ · UniProt Q3U2S8
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