pUbl depleted Parkin complex with pUbiquitin. Determined by X-ray diffraction at 3.3 Å resolution. Released 11 Sept 2024.
Explore 8IK6 in 3D Show helices and sheets RCSB PDB PDBe
8IK6 contains 20 α-helices and 66 β-strands across 4 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 | 147-150 | 4 | 15 |
| β-strand | 156-159 | 4 | 15 |
| β-strand | 160-166 | 7 | 16 |
| β-strand | 175-176 | 2 | 17 |
| α-helix | 184-187 | 4 | |
| β-strand | 193 | 1 | 18 |
| β-strand | 194-195 | 2 | 17 |
| β-strand | 205 | 1 | 18 |
| β-strand | 206-212 | 7 | 16 |
| β-strand | 224-225 | 2 | 15 |
| β-strand | 229-230 | 2 | 19 |
| α-helix | 236-238 | 3 | |
| β-strand | 248-250 | 3 | 19 |
| β-strand | 257 | 1 | 20 |
| β-strand | 258-260 | 3 | 19 |
| α-helix | 261-273 | 13 | |
| β-strand | 278-280 | 3 | 21 |
| β-strand | 284-286 | 3 | 21 |
| α-helix | 301-307 | 7 | |
| α-helix | 309-321 | 13 | |
| α-helix | 395-399 | 5 | |
| β-strand | 402 | 1 | 20 |
| β-strand | 415-417 | 3 | 22 |
| β-strand | 424-426 | 3 | 22 |
| β-strand | 431 | 1 | 23 |
| β-strand | 433-435 | 3 | 24 |
| β-strand | 444-446 | 3 | 24 |
| β-strand | 452 | 1 | 24 |
| α-helix | 455-461 | 7 | |
| β-strand | 463 | 1 | 23 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| β-strand | 2-6 | 5 | 25 |
| β-strand | 13-16 | 4 | 25 |
| β-strand | 22 | 1 | 26 |
| α-helix | 23-34 | 12 | |
| β-strand | 42-45 | 4 | 25 |
| β-strand | 48-49 | 2 | 25 |
| β-strand | 55 | 1 | 26 |
| α-helix | 61-62 | 2 | |
| β-strand | 66-70 | 5 | 25 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| β-strand | 147-150 | 4 | 1 |
| β-strand | 156-159 | 4 | 1 |
| β-strand | 160-166 | 7 | 2 |
| β-strand | 174-176 | 3 | 3 |
| α-helix | 184-187 | 4 | |
| β-strand | 193 | 1 | 4 |
| β-strand | 194-196 | 3 | 3 |
| β-strand | 205 | 1 | 4 |
| β-strand | 206-212 | 7 | 2 |
| α-helix | 222-223 | 2 | |
| β-strand | 224-225 | 2 | 1 |
| β-strand | 229-230 | 2 | 5 |
| β-strand | 237 | 1 | 6 |
| β-strand | 244 | 1 | 6 |
| β-strand | 248-250 | 3 | 5 |
| β-strand | 257 | 1 | 7 |
| β-strand | 258-260 | 3 | 5 |
| α-helix | 261-273 | 13 | |
| β-strand | 278-280 | 3 | 8 |
| β-strand | 284-286 | 3 | 8 |
| α-helix | 301-307 | 7 | |
| α-helix | 309-326 | 18 | |
| β-strand | 330-331 | 2 | 9 |
| β-strand | 340-342 | 3 | 9 |
| β-strand | 349-351 | 3 | 10 |
| β-strand | 363-365 | 3 | 10 |
| α-helix | 395-399 | 5 | |
| β-strand | 402 | 1 | 7 |
| β-strand | 417 | 1 | 11 |
| β-strand | 424 | 1 | 11 |
| β-strand | 431 | 1 | 12 |
| β-strand | 433-435 | 3 | 13 |
| β-strand | 444-446 | 3 | 13 |
| β-strand | 452 | 1 | 13 |
| α-helix | 455-461 | 7 | |
| β-strand | 463 | 1 | 12 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| β-strand | 2-7 | 6 | 9 |
| β-strand | 12-16 | 5 | 9 |
| β-strand | 22 | 1 | 14 |
| α-helix | 23-33 | 11 | |
| α-helix | 38-40 | 3 | |
| β-strand | 41-45 | 5 | 9 |
| β-strand | 48-49 | 2 | 9 |
| α-helix | 50-51 | 2 | |
| β-strand | 55 | 1 | 14 |
| α-helix | 61-62 | 2 | |
| β-strand | 66-72 | 7 | 9 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| E3 ubiquitin-protein ligase parkin | A, C | protein | 327 | Homo sapiens | O60260 (AlphaFold model) |
| Ubiquitin | B, D | protein | 75 | Homo sapiens | P62987 (AlphaFold model) |
>8IK6_1 E3 ubiquitin-protein ligase parkin (chains A, C) GPSIYNSFYVYCKGPCQRVQPGKLRVQCSTCRQATLTLTQGPSCWDDVLIPNRMSGECQS PHCPGTSAEFFFKCGAHPTSDKETSVALHLIATNSRNITCITCTDVRSPVLVFQCNSRHV ICLDCFHLYCVTRLNDRQFVHDPQLGYSLPCVAGCPNSLIKELHHFRILGEEQYNRYQQY GAEECVLQMGGVLCPRPGCGAGLLPEPDCRKVTCEGGNGLGCGFAFCRECKEAYHEGECS AVFENLYFQSQAYRVDERAAEQARWEAASKETIKKTTKPCPRCHVPVEKNGGCMHMKCPQ PQCRLEWCWNCGCEWNRVCMGDHWFDV
>8IK6_2 Ubiquitin (chains B, D) MQIFVKTLTGKTITLEVEPSDTIENVKAKIQDKEGIPPDQQRLIFAGKQLEDGRTLSDYN IQKESTLHLVLRLRG
| ID | Name | Formula | Copies |
|---|---|---|---|
| ZN | Zinc ion | Zn | 14 |
Water and common crystallization additives (SO4) are not listed.
Additional feedforward mechanism of Parkin activation via binding of phospho-UBL and RING0 in trans. Lenka, D.R., Dahe, S.V., Antico, O. et al. Elife (2024) 13. DOI 10.7554/eLife.96699 · 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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