MolNFT v1 · #152963 · protein
Structural basis for activity of tric counter-ion channels in calcium release
6IZ3 · Trimeric intracellular cation channel type B-B: “Structural basis for activity of tric counter-ion channels in calcium release”. X-ray diffraction, 15 pockets (best druggability 0.81). MolNFT v1 #152963 on GenesisL1: 3D structure…
- PDB
- 6IZ3
- Type
- protein
- Length
- 896 residues
- Chains
- 4
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Trimeric intracellular cation channel type B-B
- UniProt
- Q6GN30
- Pockets
- 15 · best druggability 0.81
Structure
x-ray diffraction · 1 distinct chain · 77% helix, 0% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, B, C, D | Trimeric intracellular cation channel type B-B | protein | 224 | 77% helix, 0% strand | Q6GN30 |
Pockets
15 pockets found on a 1 Å grid, 9 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 491 | 0.81 | 0.87 | 46 | empty |
| 2 | 377 | 0.80 | 0.88 | 35 | empty |
| 3 | 381 | 0.79 | 0.87 | 37 | empty |
| 4 | 400 | 0.65 | 0.79 | 45 | empty |
| 5 | 377 | 0.64 | 0.79 | 45 | empty |
Interfaces
4 interfaces between chains.
- A–B · 814 Ų buried · 8 hydrogen bonds · protein-protein
- B–C · 785 Ų buried · 6 hydrogen bonds · protein-protein
- A–C · 775 Ų buried · 5 hydrogen bonds · protein-protein
- B–D · 493 Ų buried · 1 hydrogen bond · protein-protein
Compared structures
- 6IZ3 · Structural basis for activity of TRIC counter-ion channels in calcium release · the same entry in another collection · chain A against A, TM-score 1.00
- Q6GN30 · AlphaFold monomer V2.0 prediction for trimeric intracellular cation channel type B-B… · a predicted model of the same protein · chain A against A, TM-score 0.99
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 Q6GN30
- Elsewhere: RCSB PDB 6IZ3 · PDBe 6IZ3 · UniProt Q6GN30
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