Research workbench
Crystal structure of KV4.3 T1 domain
Analyse Crystal structure of KV4.3 T1 domain in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 1S1G
- Type
- protein
- Length
- 217 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Potassium voltage-gated channel subfamily D member 3
- UniProt
- Q9UK17
- Ligands
- ZN
- Pockets
- 1 · best druggability 0.49
Structure
x-ray diffraction · 2 distinct chains · 47% helix, 17% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Potassium voltage-gated channel subfamily D member 3 | protein | 107 | 46% helix, 17% strand | Q9UK17 |
| B | Potassium voltage-gated channel subfamily D member 3 | protein | 110 | 47% helix, 17% strand | Q9UK17 |
Ligands and binding sites
- ZN · Zinc ion · metal · 2 copies · chains A, B
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
1 pocket found on a 1 Å grid, 0 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 72 | 0.49 | 0.84 | 19 | empty |
Interfaces
1 interface between chains.
- A–B · 987 Ų buried · 22 hydrogen bonds · protein-protein
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 Q9UK17
- Elsewhere: RCSB PDB 1S1G · PDBe 1S1G · UniProt Q9UK17
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