Research workbench
Identification of the activator binding residues in the second cysteine-rich regulatory domain of protein kinase C theta
Analyse Identification of the activator binding residues in the second cysteine-rich… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 4FKD
- Type
- protein
- Length
- 65 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Protein kinase C theta type
- EC
- 2.7.11.13
- UniProt
- Q02111
- Ligands
- ZN
Structure
x-ray diffraction · 1 distinct chain · 9% helix, 37% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Protein kinase C theta type (EC 2.7.11.13) | protein | 65 | 9% helix, 37% strand | Q02111 |
Ligands and binding sites
- ZN · Zinc ion · metal · 2 copies · chains A
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Compared structures
- 4FKD · Identification of the Activator Binding Residues in the Second Cysteine-Rich Regulatory… · the same entry in another collection · chain A against A, TM-score 1.00
- Q02111 · AlphaFold monomer V2.0 prediction for protein kinase C theta type (Q02111) · a predicted model of the same protein · chain A against A, TM-score 0.80
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 Q02111
- Elsewhere: RCSB PDB 4FKD · PDBe 4FKD · UniProt Q02111
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