MolNFT v1 · #30931 · protein
Crystal structures of the mthk rck domain in CA2+ bound form
2AEF · Calcium-gated potassium channel mthk: “Crystal structures of the mthk rck domain in CA2+ bound form”. X-ray diffraction, 1 ligand (CA), 7 pockets (best druggability 0.67). MolNFT v1 #30931 on GenesisL1: 3D structure, binding sites…
- PDB
- 2AEF
- Type
- protein
- Length
- 440 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Calcium-gated potassium channel mthk
- UniProt
- O27564
- Ligands
- CA
- Pockets
- 7 · best druggability 0.67
Structure
x-ray diffraction · 2 distinct chains · 40% helix, 24% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Calcium-gated potassium channel mthk | protein | 221 | 40% helix, 24% strand | O27564 |
| B | Calcium-gated potassium channel mthk | protein | 219 | 39% helix, 23% strand | O27564 |
Ligands and binding sites
- CA · Calcium ion · metal · 2 copies · chains A, B
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
7 pockets found on a 1 Å grid, 2 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 345 | 0.67 | 0.81 | 32 | empty |
| 2 | 151 | 0.58 | 0.83 | 29 | empty |
| 3 | 178 | 0.45 | 0.75 | 22 | empty |
| 4 | 110 | 0.38 | 0.75 | 21 | empty |
| 5 | 126 | 0.38 | 0.74 | 26 | empty |
Interfaces
1 interface between chains.
- A–B · 3376 Ų buried · 42 hydrogen bonds · protein-protein
Compared structures
- 2AEF · Crystal Structures of the MthK RCK Domain in Ca2+ bound form · the same entry in another collection · chain A against A, TM-score 1.00
- O27564 · AlphaFold monomer V2.0 prediction for calcium-gated potassium channel mthk (O27564) · a predicted model of the same protein · chain B against A, TM-score 0.94
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 O27564
- Elsewhere: RCSB PDB 2AEF · PDBe 2AEF · UniProt O27564
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