Research workbench
Pseudo-atomic model of the camkiia holoenzyme.
Analyse Pseudo-atomic model of the camkiia holoenzyme. in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 5U6Y
- Type
- protein
- Length
- 5,508 residues
- Chains
- 12
- Method
- electron microscopy
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- CALCIUM/CALMODULIN-dependent protein kinase type II subunit alpha
- EC
- 2.7.11.17
- UniProt
- P11275
- Pockets
- 20 · best druggability 0.80
Structure
electron microscopy · 1 distinct chain · 34% helix, 24% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, B, C, D, E, F, G, H, I, J, K, L | CALCIUM/CALMODULIN-dependent protein kinase type II subunit alpha (EC 2.7.11.17) | protein | 459 | 34% helix, 24% strand | P11275 |
Pockets
20 pockets found on a 1 Å grid, 20 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 1042 | 0.80 | 0.81 | 78 | empty |
| 2 | 1101 | 0.78 | 0.80 | 90 | empty |
| 3 | 1021 | 0.78 | 0.80 | 84 | empty |
| 4 | 1063 | 0.78 | 0.80 | 76 | empty |
| 5 | 923 | 0.75 | 0.78 | 80 | empty |
Interfaces
30 interfaces between chains.
- E–G · 1380 Ų buried · 12 hydrogen bonds · protein-protein
- D–J · 1264 Ų buried · 13 hydrogen bonds · protein-protein
- F–K · 1257 Ų buried · 13 hydrogen bonds · protein-protein
- B–I · 1245 Ų buried · 12 hydrogen bonds · protein-protein
- C–H · 1228 Ų buried · 12 hydrogen bonds · protein-protein
Compared structures
- 5U6Y · Pseudo-atomic model of the CaMKIIa holoenzyme. · the same entry in another collection · chain L against L, 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 P11275
- Elsewhere: RCSB PDB 5U6Y · PDBe 5U6Y · UniProt P11275
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