Structure of PKC in Complex with a Substrate Peptide from Par-3. Determined by X-ray diffraction at 2.4 Å resolution. Released 11 Jul 2012.
Explore 4DC2 in 3D Show helices and sheets RCSB PDB PDBe
4DC2 contains 21 α-helices and 16 β-strands across 2 chains. Residue ranges use author residue numbering, as in the PDB file, from PDBe. To see them in 3D, choose the Cartoon representation with Secondary structure coloring: helices, sheets and coils get different colors.
| Element | Residues | Length | Sheet |
|---|---|---|---|
| α-helix | 241-243 | 3 | |
| β-strand | 244-252 | 9 | 1 |
| β-strand | 256-263 | 8 | 1 |
| β-strand | 268-276 | 9 | 1 |
| α-helix | 277-279 | 3 | |
| α-helix | 288-299 | 12 | |
| β-strand | 305 | 1 | 2 |
| α-helix | 306-307 | 2 | |
| β-strand | 308-313 | 6 | 1 |
| β-strand | 317-323 | 7 | 1 |
| β-strand | 329 | 1 | 2 |
| α-helix | 330-337 | 8 | |
| α-helix | 342-361 | 20 | |
| β-strand | 365 | 1 | 3 |
| α-helix | 371-373 | 3 | |
| β-strand | 374-376 | 3 | 2 |
| β-strand | 382-384 | 3 | 2 |
| β-strand | 391 | 1 | 3 |
| α-helix | 394-395 | 2 | |
| β-strand | 400 | 1 | 4 |
| β-strand | 405 | 1 | 5 |
| α-helix | 407-409 | 3 | |
| α-helix | 412-415 | 4 | |
| β-strand | 420 | 1 | 4 |
| α-helix | 423-438 | 16 | |
| α-helix | 457-466 | 10 | |
| α-helix | 467-469 | 3 | |
| α-helix | 477-486 | 10 | |
| α-helix | 502-508 | 7 | |
| α-helix | 517-521 | 5 | |
| α-helix | 526-527 | 2 | |
| α-helix | 539-541 | 3 | |
| α-helix | 544-547 | 4 | |
| α-helix | 558-561 | 4 | |
| α-helix | 566-569 | 4 | |
| β-strand | 574-575 | 2 | 1 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| β-strand | 1061 | 1 | 5 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| Protein kinase C iota type | A | protein | 396 | Mus musculus | Q62074 (AlphaFold model) |
| Partitioning defective 3 homolog | Z | protein | 28 | Rattus norvegicus | Q9Z340 (AlphaFold model) |
>4DC2_1 Protein kinase C iota type (chains A) MSYYHHHHHHDYDIPTTENLYFQGAMGSGIEEEKEAMNTRESGKASSSLGLQDFDLLRVI GRGSYAKVLLVRLKKTDRIYAMRVVKKELVNDDEDIDWVQTEKHVFEQASNHPFLVGLHS CFQTESRLFFVIEYVNGGDLMFHMQRQRKLPEEHARFYSAEISLALNYLHERGIIYRDLK LDNVLLDSEGHIKLTDYGMCKEGLRPGDTTSTFCGTPNYIAPEILRGEDYGFSVDWWALG VLMFEMMAGRSPFDIVGSSDNPDQNTEDYLFQVILEKQIRIPRSLSVKAASVLKSFLNKD PKERLGCHPQTGFADIQGHPFFRNVDWDMMEQKQVVPPFKPNISGEFGLDNFDSQFTNEP VQLTPDDDDIVRKIDQSEFEGFEYINPLLMSAEECV
>4DC2_2 Partitioning defective 3 homolog (chains Z) DPVLAFQREGFGRQSMSEKRTKQFSNAS
| ID | Name | Formula | Copies |
|---|---|---|---|
| ADE | Adenine | C5 H5 N5 | 1 |
Substrate recognition mechanism of atypical protein kinase Cs revealed by the structure of PKC iota in complex with a substrate peptide from Par-3. Wang, C., Shang, Y., Yu, J. et al. Structure (2012) 20:791-801. DOI 10.1016/j.str.2012.02.022 · PubMed
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