Research workbench
Crystal structure of pas domain from the fruit-fly elk potassium channel
Analyse Crystal structure of pas domain from the fruit-fly elk potassium channel in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 4HP4
- Type
- protein
- Length
- 249 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Eag-like K[+] channel
- EC
- 2.7.3.-
- UniProt
- A1ZB14
- Ligands
- SO4
- Pockets
- 3 · best druggability 0.72
Structure
x-ray diffraction · 2 distinct chains · 27% helix, 33% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Eag-like K[+] channel (EC 2.7.3.-) | protein | 123 | 28% helix, 33% strand | A1ZB14 |
| B | Eag-like K[+] channel (EC 2.7.3.-) | protein | 126 | 27% helix, 33% strand | A1ZB14 |
Ligands and binding sites
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
3 pockets found on a 1 Å grid, 1 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 93 | 0.72 | 0.94 | 22 | empty |
| 2 | 180 | 0.47 | 0.76 | 31 | SO4, GOL |
| 3 | 85 | 0.35 | 0.75 | 16 | empty |
Interfaces
1 interface between chains.
- A–B · 866 Ų buried · 13 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 23 modified (methylation).
Compared structures
- 4HP4 · Crystal structure of PAS domain from the fruit-fly ELK potassium channel · 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 A1ZB14
- Elsewhere: RCSB PDB 4HP4 · PDBe 4HP4 · UniProt A1ZB14
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