Research workbench
The structure of the ef-hand domain of polycystin-2 suggests a mechanism for CA2+-dependent regulation of polycystin-2 channel activity
Analyse The structure of the ef-hand domain of polycystin-2 suggests a mechanism for… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 2KQ6
- Type
- protein
- Length
- 78 residues
- Chains
- 1
- Method
- solution nmr
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Polycystin-2
- UniProt
- Q13563
Structure
solution nmr · 1 distinct chain · 58% helix, 0% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Polycystin-2 | protein | 78 | 58% helix, 0% strand | Q13563 |
Compared structures
- 2KQ6 · The structure of the EF-hand domain of polycystin-2 suggests a mechanism for… · the same entry in another collection · chain A against A, TM-score 1.00
- Q13563 · AlphaFold monomer V2.0 prediction for polycystin-2 (Q13563) · a predicted model of the same protein · chain A against A, TM-score 0.60
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 Q13563
- Elsewhere: RCSB PDB 2KQ6 · PDBe 2KQ6 · UniProt Q13563
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