Research workbench
KIRBAC3.1 mutant at a resolution of 3.1 ångströms
Analyse KIRBAC3.1 mutant at a resolution of 3.1 ångströms in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 6O9V
- Type
- protein
- Length
- 561 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Inward rectifier potassium channel KIRBAC3.1
- UniProt
- D9N164
- Ligands
- TMO, DDQ, M1M, K
- Pockets
- 5 · best druggability 0.77
Structure
x-ray diffraction · 2 distinct chains · 30% helix, 32% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Inward rectifier potassium channel KIRBAC3.1 | protein | 279 | 30% helix, 32% strand | D9N164 |
| B | Inward rectifier potassium channel KIRBAC3.1 | protein | 282 | 29% helix, 32% strand | D9N164 |
Ligands and binding sites
- TMO · trimethylamine oxide · ligand · 2 copies · chains A, B
- DDQ · Decylamine-N,N-dimethyl-N-oxide · ligand · 2 copies · chains A, B
- M1M · 1,1-Methanediyl Bismethanethiosulfonate · ligand · 2 copies · chains A, B
- K · Potassium ion · metal · 3 copies · chains A, B
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
5 pockets found on a 1 Å grid, 2 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 564 | 0.77 | 0.84 | 55 | DDQ |
| 2 | 143 | 0.60 | 0.84 | 19 | empty |
| 3 | 148 | 0.44 | 0.75 | 16 | empty |
| 4 | 88 | 0.34 | 0.75 | 14 | empty |
| 5 | 53 | 0.32 | 0.77 | 16 | empty |
Interfaces
1 interface between chains.
- A–B · 2484 Ų buried · 30 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 3 covalent (covalent ligand).
Compared structures
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 D9N164
- Elsewhere: RCSB PDB 6O9V · PDBe 6O9V · UniProt D9N164
GL1X is a live explorer of the GenesisL1 blockchain. Turn on JavaScript for search, charts and interactive views.