Research workbench
C2 domain from protein kinase C (alpha) complexed with CA2+ and phosphatidylserine
Analyse C2 domain from protein kinase C (alpha) complexed with CA2+ and… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 1DSY
- Type
- protein
- Length
- 137 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Protein kinase C, alpha type
- EC
- 2.7.1.-
- UniProt
- P05696
- Ligands
- PSF, CA, PO4
Structure
x-ray diffraction · 1 distinct chain · 9% helix, 47% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Protein kinase C, alpha type (EC 2.7.1.-) | protein | 137 | 9% helix, 47% strand | P05696 |
Ligands and binding sites
- PSF · 1,2-dicaproyl-sn-phosphatidyl-L-serine · ligand · chains A
- CA · Calcium ion · metal · 2 copies · chains A
- PO4 · Phosphate ion · ion · chains A
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Compared structures
- 1DSY · C2 domain from protein kinase C (alpha) complexed with CA2+ and phosphatidylserine · the same entry in another collection · chain A against A, TM-score 1.00
- P05696 · AlphaFold monomer V2.0 prediction for protein kinase C alpha type (P05696) · a predicted model of the same protein · chain A against A, TM-score 0.98
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 P05696
- Elsewhere: RCSB PDB 1DSY · PDBe 1DSY · UniProt P05696
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