MolNFT v1 · #170316 · protein
14-3-3 sigma in complex with phosphorylated CAMKK2 peptide
6Y3O · 14-3-3 protein sigma: “14-3-3 sigma in complex with phosphorylated CAMKK2 peptide”. X-ray diffraction, 2 ligands (MG, CA), 1 pocket (best druggability 0.52). MolNFT v1 #170316 on GenesisL1: 3D structure, binding sites and pockets in…
- PDB
- 6Y3O
- Type
- protein
- Length
- 239 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- 14-3-3 protein sigma; CAMKK2
- UniProt
- P31947
- Ligands
- MG, CA
- Pockets
- 1 · best druggability 0.52
Structure
x-ray diffraction · 2 distinct chains · 78% helix, 0% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | 14-3-3 protein sigma | protein | 234 | 80% helix, 0% strand | P31947 |
| P | CAMKK2 | protein | 5 | 0% helix, 0% strand | — |
Ligands and binding sites
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
1 pocket found on a 1 Å grid, 1 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 161 | 0.52 | 0.79 | 24 | empty |
Interfaces
1 interface between chains.
- A–P · 375 Ų buried · 9 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 2 modified (oxidation, phosphorylation).
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 P31947
- Elsewhere: RCSB PDB 6Y3O · PDBe 6Y3O · UniProt P31947
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