Research workbench
Ion selectivity in a semi-synthetic K+ channel locked in the conductive conformation
Analyse Ion selectivity in a semi-synthetic K+ channel locked in the conductive… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 2IH1
- Type
- protein
- Length
- 532 residues
- Chains
- 3
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Fab heavy chain; Fab light chain; Voltage-gated potassium channel
- UniProt
- P0A334
- Ligands
- 1EM, K
- Pockets
- 5 · best druggability 0.68
Structure
x-ray diffraction · 3 distinct chains · 18% helix, 41% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Fab heavy chain | protein | 219 | 4% helix, 50% strand | — |
| B | Fab light chain | protein | 212 | 6% helix, 51% strand | — |
| C | Voltage-gated potassium channel | protein | 101 | 75% helix, 0% strand | P0A334 |
Ligands and binding sites
- 1EM · (1S)-2-hydroxy-1-[(nonanoyloxy)methyl]ethyl myristate · ligand · chains C
- K · Potassium ion · metal · 5 copies · chains C
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
5 pockets found on a 1 Å grid, 3 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 727 | 0.68 | 0.76 | 59 | empty |
| 2 | 74 | 0.52 | 0.86 | 17 | empty |
| 3 | 68 | 0.51 | 0.85 | 16 | empty |
| 4 | 125 | 0.49 | 0.80 | 25 | empty |
| 5 | 92 | 0.37 | 0.75 | 18 | empty |
Interfaces
3 interfaces between chains.
- A–B · 1838 Ų buried · 19 hydrogen bonds · protein-protein
- A–C · 500 Ų buried · 10 hydrogen bonds · protein-protein
- B–C · 438 Ų buried · 8 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 3 disulfide, 1 d-amino (disulfide, D-amino acid).
Compared structures
- 2IH1 · Ion selectivity in a semi-synthetic K+ channel locked in the conductive conformation · the same entry in another collection · chain A against A, TM-score 1.00
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 P0A334
- Elsewhere: RCSB PDB 2IH1 · PDBe 2IH1 · UniProt P0A334
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