Crystal Structure of the Catalytic Domain of Atypical Protein Kinase C-iota. Determined by X-ray diffraction at 3.0 Å resolution. Released 13 Sept 2005.
Explore 1ZRZ in 3D Show helices and sheets RCSB PDB PDBe
1ZRZ contains 19 α-helices and 15 β-strands across 1 chain. 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 |
|---|---|---|---|
| β-strand | 245-253 | 9 | 1 |
| β-strand | 257-264 | 8 | 1 |
| β-strand | 270-277 | 8 | 1 |
| α-helix | 278-280 | 3 | |
| α-helix | 287-297 | 11 | |
| β-strand | 306 | 1 | 2 |
| β-strand | 309-312 | 4 | 1 |
| β-strand | 314 | 1 | 1 |
| β-strand | 318-324 | 7 | 1 |
| β-strand | 330 | 1 | 2 |
| α-helix | 331-336 | 6 | |
| α-helix | 343-362 | 20 | |
| β-strand | 366 | 1 | 3 |
| α-helix | 372-374 | 3 | |
| β-strand | 375-377 | 3 | 2 |
| α-helix | 378 | 1 | |
| β-strand | 383-385 | 3 | 2 |
| β-strand | 392 | 1 | 3 |
| β-strand | 401 | 1 | 4 |
| α-helix | 408-410 | 3 | |
| α-helix | 413-416 | 4 | |
| β-strand | 421 | 1 | 4 |
| α-helix | 424-439 | 16 | |
| α-helix | 457-467 | 11 | |
| α-helix | 469-473 | 5 | |
| α-helix | 478-487 | 10 | |
| α-helix | 503-509 | 7 | |
| α-helix | 511-513 | 3 | |
| α-helix | 518-521 | 4 | |
| α-helix | 527-528 | 2 | |
| α-helix | 553-557 | 5 | |
| α-helix | 559-562 | 4 | |
| α-helix | 568-570 | 3 | |
| β-strand | 575-576 | 2 | 1 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| Protein kinase C, iota | A | protein | 364 | Homo sapiens | P41743 (AlphaFold model) |
>1ZRZ_1 Protein kinase C, iota (chains A) EKEAMNTRESGKASSSLGLQDFDLLRVIGRGSYAKVLLVRLKKTDRIYAMKVVKKELVND DEDIDWVQTEKHVFEQASNHPFLVGLHSCFQTESRLFFVIEYVNGGDLMFHMQRQRKLPE EHARFYSAEISLALNYLHERGIIYRDLKLDNVLLDSEGHIKLTDYGMCKEGLRPGDTTST FCGTPNYIAPEILRGEDYGFSVDWWALGVLMFEMMAGRSPFDIVGSSDNPDQNTEDYLFQ VILEKQIRIPRSMSVKAASVLKSFLNKDPKERLGCLPQTGFADIQGHPFFRNVDWDMMEQ KQVVPPFKPNISGEFGLDNFDSQFTNERVQLTPDDDDIVRKIDQSEFEGFEYINPLLMSA EECV
| ID | Name | Formula | Copies |
|---|---|---|---|
| BI1 | 3-{1-[3-(dimethylamino)propyl]-1H-indol-3-yl}-4-(1H-indol-3-yl)-1H-pyrrole-2,5-… | C25 H24 N4 O2 | 1 |
Crystal Structure of the Catalytic Domain of Human Atypical Protein Kinase C-iota Reveals Interaction Mode of Phosphorylation Site in Turn Motif. Messerschmidt, A., Macieira, S., Velarde, M. et al. J Mol Biol (2005) 352:918-931. DOI 10.1016/j.jmb.2005.07.060 · PubMed
Other PDB entries of the same protein (UniProt P41743 (AlphaFold model), which also has an AlphaFold model), best resolution first:
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