Crystal Structure of a threonine-selective RCR E3 ligase. Determined by X-ray diffraction at 1.75 Å resolution. Released 18 Apr 2018.
Explore 5O6C in 3D Show helices and sheets RCSB PDB PDBe
5O6C contains 20 α-helices and 19 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 |
|---|---|---|---|
| α-helix | 4388 | 1 | |
| β-strand | 4389 | 1 | 1 |
| α-helix | 4390 | 1 | |
| β-strand | 4397 | 1 | 1 |
| α-helix | 4398-4400 | 3 | |
| β-strand | 4403-4405 | 3 | 2 |
| β-strand | 4411-4413 | 3 | 2 |
| α-helix | 4414-4423 | 10 | |
| α-helix | 4433-4435 | 3 | |
| β-strand | 4436 | 1 | 3 |
| β-strand | 4443 | 1 | 3 |
| α-helix | 4444 | 1 | |
| α-helix | 4447-4449 | 3 | |
| α-helix | 4450-4473 | 24 | |
| α-helix | 4480-4483 | 4 | |
| α-helix | 4493-4500 | 8 | |
| β-strand | 4501-4505 | 5 | 4 |
| β-strand | 4512-4517 | 6 | 4 |
| α-helix | 4532-4534 | 3 | |
| β-strand | 4535 | 1 | 5 |
| α-helix | 4539-4541 | 3 | |
| α-helix | 4546-4548 | 3 | |
| β-strand | 4549 | 1 | 6 |
| β-strand | 4553 | 1 | 6 |
| β-strand | 4557-4559 | 3 | 7 |
| β-strand | 4560 | 1 | 8 |
| β-strand | 4567 | 1 | 8 |
| β-strand | 4570-4572 | 3 | 5 |
| β-strand | 4576-4578 | 3 | 5 |
| α-helix | 4580-4584 | 5 | |
| α-helix | 4586-4591 | 6 | |
| α-helix | 4594-4596 | 3 | |
| α-helix | 4598-4599 | 2 | |
| β-strand | 4602-4603 | 2 | 9 |
| α-helix | 4604-4606 | 3 | |
| β-strand | 4607-4608 | 2 | 9 |
| α-helix | 4621-4622 | 2 | |
| β-strand | 4628-4631 | 4 | 7 |
| α-helix | 4634-4636 | 3 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| E3 ubiquitin-protein ligase MYCBP2 | A | protein | 263 | Homo sapiens | O75592 |
>5O6C_1 E3 ubiquitin-protein ligase MYCBP2 (chains A) SATSLKQDADDMCMICFTEALSAAPAIQLDCSHIFHLQCCRRVLENRWLGPRITFGFISC PICKNKINHIVLKDLLDPIKELYEDVRRKALMRLEYEGLHKSEAITTPGVRFYNDPAGYA MNRYAYYVCYKCRKAYFGGEARCDAEAGRGDDYDPRELICGACSDVSRAQMCPKHGTDFL EYKCRYCCSVAVFFCFGTTHFCNACHDDFQRMTSIPKEELPHCPAGPKGKQLEGTECPLH VVHPPTGEEFALGCGVCRNAHTF
| ID | Name | Formula | Copies |
|---|---|---|---|
| ZN | Zinc ion | Zn | 6 |
Activity-based E3 ligase profiling uncovers an E3 ligase with esterification activity. Pao, K.C., Wood, N.T., Knebel, A. et al. Nature (2018) 556:381-385. DOI 10.1038/s41586-018-0026-1 · PubMed
Other PDB entries of the same protein (UniProt O75592), best resolution first:
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