ParkinS65N. Determined by X-ray diffraction at 2.85 Å resolution. Released 17 Oct 2018.
Explore 6HUE in 3D Show helices and sheets RCSB PDB PDBe
6HUE contains 28 α-helices and 72 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 |
|---|---|---|---|
| β-strand | 2-7 | 6 | 1 |
| β-strand | 13-16 | 4 | 1 |
| β-strand | 22 | 1 | 2 |
| α-helix | 23-34 | 12 | |
| α-helix | 38-40 | 3 | |
| β-strand | 41-45 | 5 | 1 |
| β-strand | 48-50 | 3 | 1 |
| α-helix | 51 | 1 | |
| β-strand | 55 | 1 | 2 |
| β-strand | 66-71 | 6 | 1 |
| β-strand | 147-150 | 4 | 3 |
| β-strand | 156-159 | 4 | 3 |
| β-strand | 160-166 | 7 | 4 |
| β-strand | 174-176 | 3 | 5 |
| α-helix | 183-187 | 5 | |
| β-strand | 193 | 1 | 6 |
| β-strand | 194-196 | 3 | 5 |
| β-strand | 205 | 1 | 6 |
| β-strand | 206-212 | 7 | 4 |
| β-strand | 224-225 | 2 | 3 |
| β-strand | 229-230 | 2 | 7 |
| α-helix | 236-238 | 3 | |
| β-strand | 248-250 | 3 | 7 |
| α-helix | 251 | 1 | |
| β-strand | 257 | 1 | 8 |
| β-strand | 258-260 | 3 | 7 |
| α-helix | 261-274 | 14 | |
| β-strand | 278-280 | 3 | 9 |
| β-strand | 284-286 | 3 | 9 |
| α-helix | 301-307 | 7 | |
| α-helix | 308-316 | 9 | |
| α-helix | 318-327 | 10 | |
| β-strand | 330-331 | 2 | 10 |
| β-strand | 340-341 | 2 | 10 |
| β-strand | 349-351 | 3 | 11 |
| β-strand | 363-365 | 3 | 11 |
| β-strand | 371 | 1 | 11 |
| α-helix | 395-400 | 6 | |
| β-strand | 402 | 1 | 8 |
| β-strand | 415-417 | 3 | 12 |
| β-strand | 424-426 | 3 | 12 |
| β-strand | 431 | 1 | 13 |
| β-strand | 433-435 | 3 | 14 |
| β-strand | 444-446 | 3 | 14 |
| β-strand | 452 | 1 | 14 |
| α-helix | 455-461 | 7 | |
| β-strand | 463 | 1 | 13 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| β-strand | 2-6 | 5 | 15 |
| α-helix | 12 | 1 | |
| β-strand | 13-16 | 4 | 15 |
| β-strand | 22 | 1 | 16 |
| α-helix | 23-34 | 12 | |
| α-helix | 38-40 | 3 | |
| β-strand | 41-45 | 5 | 15 |
| β-strand | 48-50 | 3 | 15 |
| α-helix | 51 | 1 | |
| β-strand | 55 | 1 | 16 |
| β-strand | 66-71 | 6 | 15 |
| β-strand | 147-150 | 4 | 17 |
| β-strand | 156-159 | 4 | 17 |
| β-strand | 160-166 | 7 | 18 |
| β-strand | 174-176 | 3 | 19 |
| α-helix | 183-187 | 5 | |
| β-strand | 193 | 1 | 20 |
| β-strand | 194-196 | 3 | 19 |
| β-strand | 205 | 1 | 20 |
| β-strand | 206-212 | 7 | 18 |
| β-strand | 224-225 | 2 | 17 |
| β-strand | 229-230 | 2 | 21 |
| α-helix | 236 | 1 | |
| β-strand | 237 | 1 | 22 |
| α-helix | 238 | 1 | |
| β-strand | 244 | 1 | 22 |
| β-strand | 248-250 | 3 | 21 |
| α-helix | 251 | 1 | |
| β-strand | 257 | 1 | 23 |
| β-strand | 258-260 | 3 | 21 |
| α-helix | 261-274 | 14 | |
| α-helix | 277 | 1 | |
| β-strand | 278-280 | 3 | 24 |
| β-strand | 284-286 | 3 | 24 |
| α-helix | 301-307 | 7 | |
| α-helix | 309-316 | 8 | |
| α-helix | 318-326 | 9 | |
| β-strand | 330-331 | 2 | 25 |
| β-strand | 340-341 | 2 | 25 |
| β-strand | 349-350 | 2 | 26 |
| β-strand | 364-365 | 2 | 26 |
| β-strand | 371 | 1 | 26 |
| α-helix | 377-378 | 2 | |
| α-helix | 395-400 | 6 | |
| β-strand | 402 | 1 | 23 |
| β-strand | 415-417 | 3 | 27 |
| β-strand | 424-426 | 3 | 27 |
| β-strand | 431 | 1 | 28 |
| β-strand | 433-435 | 3 | 29 |
| β-strand | 444-446 | 3 | 29 |
| β-strand | 452 | 1 | 29 |
| α-helix | 455-461 | 7 | |
| β-strand | 463 | 1 | 28 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| E3 ubiquitin-protein ligase parkin | A, B | protein | 405 | Homo sapiens | O60260 (AlphaFold model) |
>6HUE_1 E3 ubiquitin-protein ligase parkin (chains A, B) MIVFVRFNSSHGFPVEVDSDTSIFQLKEVVAKRQGVPADQLRVIFAGKELRNDWTVQNCD LDQQNIVHIVQRPWRKGQEMNATNSFYVYCKGPCQRVQPGKLRVQCSTCRQATLTLTQGP SCWDDVLIPNRMSGECQSPHCPGTSAEFFFKCGAHPTSDKETSVALHLIATNSRNITCIT CTDVRSPVLVFQCNSRHVICLDCFHLYCVTRLNDRQFVHDPQLGYSLPCVAGCPNSLIKE LHHFRILGEEQYNRYQQYGAEECVLQMGGVLCPRPGCGAGLLPEPDQRKVTCEGGNGLGC GFAFCRECKEAYHEGECSAVFEASGTTTQAYRVDERAAEQARWEAASKETIKKTTKPCPR CHVPVEKNGGCMHMKCPQPQCRLEWCWNCGCEWNRVCMGDHWFDV
| ID | Name | Formula | Copies |
|---|---|---|---|
| ZN | Zinc ion | Zn | 16 |
Water and common crystallization additives (CL, GOL, SO4) are not listed.
Phosphorylation of Parkin at serine 65 is essential for its activation in vivo . McWilliams, T.G., Barini, E., Pohjolan-Pirhonen, R. et al. Open Biol (2018) 8. DOI 10.1098/rsob.180108 · PubMed
Other PDB entries of the same protein (UniProt O60260 (AlphaFold model), which also has an AlphaFold model), best resolution first:
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