Research workbench
Structural and functional characterization of an anesthetic binding site in the second cysteine-rich domain of protein kinase cdelta
Analyse Structural and functional characterization of an anesthetic binding site in the… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 3UFF
- Type
- protein
- Length
- 130 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Protein kinase C delta type
- EC
- 2.7.11.13
- UniProt
- P28867
- Ligands
- ZN, PO4
Structure
x-ray diffraction · 1 distinct chain · 6% helix, 34% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, B | Protein kinase C delta type (EC 2.7.11.13) | protein | 65 | 6% helix, 34% strand | P28867 |
Ligands and binding sites
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Interfaces
1 interface between chains.
- A–B · 461 Ų buried · 13 hydrogen bonds · protein-protein
Compared structures
- 3UFF · Structural and functional characterization of an anesthetic binding site in the second… · the same entry in another collection · chain A against A, TM-score 1.00
- P28867 · AlphaFold monomer V2.0 prediction for protein kinase C delta type (P28867) · a predicted model of the same protein · chain A against A, TM-score 0.77
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 P28867
- Elsewhere: RCSB PDB 3UFF · PDBe 3UFF · UniProt P28867
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