MolNFT v1 · #172787 · protein
KIRBAC3.1 W46R: role of a highly conserved tryptophan at the membrane- water interface of kir channel
7ADI · Inward rectifier potassium channel KIRBAC3.1: “KIRBAC3.1 W46R: role of a highly conserved tryptophan at the membrane- water interface of kir channel”. X-ray diffraction, 2 ligands (K, MG), 4 pockets (best druggability 0.77). MolNFT…
- PDB
- 7ADI
- Type
- protein
- Length
- 541 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
- K, MG
- Pockets
- 4 · 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 | 276 | 30% helix, 31% strand | D9N164 |
| B | Inward rectifier potassium channel KIRBAC3.1 | protein | 265 | 30% helix, 33% strand | D9N164 |
Ligands and binding sites
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
4 pockets found on a 1 Å grid, 3 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 403 | 0.77 | 0.86 | 44 | empty |
| 2 | 833 | 0.71 | 0.76 | 86 | empty |
| 3 | 186 | 0.61 | 0.82 | 25 | empty |
| 4 | 73 | 0.40 | 0.79 | 18 | empty |
Interfaces
1 interface between chains.
- A–B · 2440 Ų buried · 23 hydrogen bonds · protein-protein
Compared structures
- 7ADI · KirBac3.1 W46R: role of a highly conserved tryptophan at the membrane-water interface of… · the same entry in another collection · chain A against A, TM-score 1.00
- D9N164 · AlphaFold monomer V2.0 prediction for inward rectifier potassium channel KIRBAC3.1… · a predicted model of the same protein · chain B against A, TM-score 0.93
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 7ADI · PDBe 7ADI · UniProt D9N164
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