Research workbench
Cask cam-kinase domain- amppnp complex, P1 form
Analyse Cask cam-kinase domain- amppnp complex, P1 form in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 3C0H
- Type
- protein
- Length
- 600 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Peripheral plasma membrane protein cask
- EC
- 2.7.11.1
- UniProt
- O14936
- Ligands
- AMP
- Pockets
- 7 · best druggability 0.72
Structure
x-ray diffraction · 1 distinct chain · 44% helix, 18% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, B | Peripheral plasma membrane protein cask (EC 2.7.11.1) | protein | 300 | 44% helix, 18% strand | O14936 |
Ligands and binding sites
- AMP · Adenosine monophosphate · ligand · 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, 3 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 568 | 0.72 | 0.80 | 49 | AMP |
| 2 | 574 | 0.71 | 0.79 | 51 | AMP |
| 3 | 356 | 0.60 | 0.77 | 38 | empty |
| 4 | 91 | 0.42 | 0.79 | 20 | empty |
| 5 | 125 | 0.40 | 0.74 | 22 | empty |
Interfaces
1 interface between chains.
- A–B · 538 Ų buried · 13 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 O14936
- Elsewhere: RCSB PDB 3C0H · PDBe 3C0H · UniProt O14936
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