Research workbench
The dynamic nature of the VDAC1 channels in bilayers: human VDAC1 at 3.3 ångström resolution
Analyse The dynamic nature of the VDAC1 channels in bilayers: human VDAC1 at 3.3… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 6G73
- Type
- protein
- Length
- 1,126 residues
- Chains
- 4
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- UniProt
- P21796
- Ligands
- MC3
Structure
x-ray diffraction · 2 distinct chains.
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, D | — | protein | 282 | — | P21796 |
| B, C | — | protein | 281 | — | P21796 |
Ligands and binding sites
- MC3 · 1,2-dimyristoyl-rac-glycero-3-phosphocholine · ligand · 5 copies · chains A, B, C, D
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Compared structures
- 6G73 · The dynamic nature of the VDAC1 channels in bilayers: human VDAC1 at 3.3 Angstrom… · the same entry in another collection · chain A against A, TM-score 1.00
- P21796 · AlphaFold monomer V2.0 prediction for voltage-dependent anion- selective channel protein… · a predicted model of the same protein · chain B against A, TM-score 0.97
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 P21796
- Elsewhere: RCSB PDB 6G73 · PDBe 6G73 · UniProt P21796
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