MolNFT v2 · #220386 · protein
Cryo-EM structure of tetradecameric hub domain of CaMKII alpha
8SYG · Venus-tagged CaMKII Alpha Association Domain: “Cryo-EM structure of tetradecameric hub domain of CaMKII alpha”. Electron microscopy at 2.6, 20 pockets (best druggability 0.73). MolNFT v2 #220386 on GenesisL1: 3D structure, binding…
- PDB
- 8SYG
- Type
- protein
- Length
- 1,876 residues
- Chains
- 14
- Method
- electron microscopy
- Collection
- MolNFT v2 / PDB Bank
- Contract
- 0xd58B01f6C18086e5202cdC5D7Ad3E41790360102
- Owner
- 0xF4e1AA6f26B7DA48EeAD9B24a97927303eeA07b8
- Resolution
- 2.6
- Source
- Aequorea victoria; Rattus norvegicus
- Molecule
- Venus-tagged CaMKII Alpha Association Domain
- EC
- 2.7.11.17
- UniProt
- P42212, P11275
- Pockets
- 20 · best druggability 0.73
Structure
electron microscopy · resolution 2.6 · 1 distinct chain · 29% helix, 46% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| B, A, C, D, E, F, G, H, I, J, K, L, M, N | Venus-tagged CaMKII Alpha Association Domain (EC 2.7.11.17) | protein | 134 | 29% helix, 46% strand | P42212, 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 | 77 | 0.73 | 0.97 | 16 | empty |
| 2 | 76 | 0.73 | 0.96 | 20 | empty |
| 3 | 69 | 0.73 | 0.97 | 17 | empty |
| 4 | 69 | 0.73 | 0.97 | 15 | empty |
| 5 | 321 | 0.72 | 0.85 | 48 | empty |
Interfaces
35 interfaces between chains.
- C–M · 1102 Ų buried · 17 hydrogen bonds · protein-protein
- F–J · 1102 Ų buried · 17 hydrogen bonds · protein-protein
- B–H · 1100 Ų buried · 17 hydrogen bonds · protein-protein
- D–L · 1099 Ų buried · 17 hydrogen bonds · protein-protein
- E–K · 1099 Ų buried · 17 hydrogen bonds · protein-protein
Compared structures
- P42212 · AlphaFold monomer V2.0 prediction for green fluorescent protein (P42212) · a predicted model of the same protein · chain J against A, TM-score 0.38
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 P42212
- Every structure of UniProt P11275
- Elsewhere: RCSB PDB 8SYG · PDBe 8SYG · UniProt P42212 · UniProt P11275
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