Research workbench
Crystal structure of CKIR2.2 force open mutant in complex with PI(4, 5)P2
Analyse Crystal structure of CKIR2.2 force open mutant in complex with PI(4, 5)P2 in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 6M84
- Type
- protein
- Length
- 326 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- ATP-sensitive inward rectifier potassium channel 12
- UniProt
- F1NHE9
- Ligands
- PIO, K
- Pockets
- 3 · best druggability 0.35
Structure
x-ray diffraction · 1 distinct chain · 36% helix, 27% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | ATP-sensitive inward rectifier potassium channel 12 | protein | 326 | 36% helix, 27% strand | F1NHE9 |
Ligands and binding sites
- PIO · [(2R)-2-octanoyloxy-3-[oxidanyl-[(1R,2R,3S,4R,5R,6S)-2, 3,6-tris(oxidanyl)-4,5-diphosphonooxy-cyclohexyl]oxy-phosphoryl]oxy-propyl] octanoate · ligand · chains A
- K · Potassium ion · metal · 6 copies · chains A
- LMT · Dodecyl-beta-D-maltoside · additive · chains A
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
3 pockets found on a 1 Å grid, 0 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 80 | 0.35 | 0.76 | 18 | empty |
| 2 | 65 | 0.29 | 0.74 | 24 | empty |
| 3 | 51 | 0.25 | 0.73 | 15 | empty |
Modifications
Observed in the structure: 1 disulfide (disulfide).
Compared structures
- 6M84 · Crystal structure of cKir2.2 force open mutant in complex with PI(4,5)P2 · the same entry in another collection · chain A against A, TM-score 1.00
- F1NHE9 · AlphaFold monomer V2.0 prediction for ATP-sensitive inward rectifier potassium channel 12… · 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 F1NHE9
- Elsewhere: RCSB PDB 6M84 · PDBe 6M84 · UniProt F1NHE9
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