MolNFT v1 · #75082 · protein
Crystal structure and allosteric activation of protein kinase C beta II
3PFQ · Protein kinase C beta type: “Crystal structure and allosteric activation of protein kinase C beta II”. X-ray diffraction, 3 ligands (ANP, CA, ZN), 4 pockets (best druggability 0.73). MolNFT v1 #75082 on GenesisL1: 3D structure…
- PDB
- 3PFQ
- Type
- protein
- Length
- 523 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Protein kinase C beta type
- EC
- 2.7.11.13
- UniProt
- P68403
- Ligands
- ANP, CA, ZN
- Pockets
- 4 · best druggability 0.73
Structure
x-ray diffraction · 1 distinct chain · 23% helix, 22% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Protein kinase C beta type (EC 2.7.11.13) | protein | 523 | 23% helix, 22% strand | P68403 |
Ligands and binding sites
- ANP · Phosphoaminophosphonic acid-adenylate ester · ligand · chains A
- CA · Calcium ion · metal · 3 copies · chains A
- ZN · Zinc ion · metal · 2 copies · chains A
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
4 pockets found on a 1 Å grid, 2 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 590 | 0.73 | 0.80 | 41 | ANP |
| 2 | 404 | 0.68 | 0.80 | 29 | empty |
| 3 | 82 | 0.42 | 0.79 | 19 | empty |
| 4 | 87 | 0.32 | 0.73 | 20 | empty |
Modifications
Observed in the structure: 3 modified (phosphorylation).
Compared structures
- 3PFQ · Crystal Structure and Allosteric Activation of Protein Kinase C beta II · the same entry in another collection · chain A against A, TM-score 1.00
- P68403 · AlphaFold monomer V2.0 prediction for protein kinase C beta type (P68403) · a predicted model of the same protein · chain A against A, TM-score 0.62
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 P68403
- Elsewhere: RCSB PDB 3PFQ · PDBe 3PFQ · UniProt P68403
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