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Structure of the C2 domain from novel protein kinase C epsilon

Analyse Structure of the C2 domain from novel protein kinase C epsilon in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB
1GMI
Type
protein
Length
135 residues
Chains
1
Method
x-ray diffraction
Collection
MolNFT v1 / PDB
Contract
0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner
0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule
Protein kinase C, epsilon type
UniProt
P09216
Ligands
MG

Structure

x-ray diffraction · 1 distinct chain · 6% helix, 56% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
AProtein kinase C, epsilon typeprotein1356% helix, 56% strandP09216

Ligands and binding sites

  • MG · Magnesium ion · metal · chains A

Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.

Compared structures

  • 1GMI · Structure of the c2 domain from novel protein kinase C epsilon · the same entry in another collection · chain A against A, TM-score 1.00
  • P09216 · AlphaFold monomer V2.0 prediction for protein kinase C epsilon type (P09216) · a predicted model of the same protein · chain A against A, TM-score 0.96

Analyse

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