UbcH7-Ub Complex with R0RBR Parkin and phosphoubiquitin. Determined by solution NMR. Released 28 Nov 2018.
Explore 6N13 in 3D Show helices and sheets RCSB PDB PDBe
6N13 contains 22 α-helices and 45 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 | 2-6 | 5 | 15 |
| β-strand | 12-16 | 5 | 15 |
| β-strand | 22 | 1 | 16 |
| α-helix | 23-33 | 11 | |
| β-strand | 41-45 | 5 | 17 |
| β-strand | 48-49 | 2 | 17 |
| α-helix | 50 | 1 | |
| β-strand | 55 | 1 | 16 |
| α-helix | 56-59 | 4 | |
| β-strand | 66-67 | 2 | 15 |
| β-strand | 68-71 | 4 | 17 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| β-strand | 147-149 | 3 | 1 |
| β-strand | 157-159 | 3 | 1 |
| β-strand | 160-166 | 7 | 2 |
| β-strand | 174-176 | 3 | 3 |
| α-helix | 183-187 | 5 | |
| β-strand | 193 | 1 | 4 |
| β-strand | 194-196 | 3 | 3 |
| β-strand | 205 | 1 | 4 |
| β-strand | 206-212 | 7 | 2 |
| α-helix | 223 | 1 | |
| β-strand | 224-226 | 3 | 1 |
| β-strand | 230 | 1 | 5 |
| β-strand | 248-250 | 3 | 5 |
| β-strand | 258-260 | 3 | 5 |
| α-helix | 261-274 | 14 | |
| β-strand | 278-279 | 2 | 6 |
| β-strand | 285-286 | 2 | 6 |
| α-helix | 301-306 | 6 | |
| α-helix | 309-327 | 19 | |
| β-strand | 350-351 | 2 | 7 |
| β-strand | 363-364 | 2 | 7 |
| β-strand | 371 | 1 | 7 |
| α-helix | 378-383 | 6 | |
| α-helix | 395-400 | 6 | |
| β-strand | 415-417 | 3 | 8 |
| β-strand | 424-426 | 3 | 8 |
| β-strand | 431 | 1 | 9 |
| β-strand | 433-436 | 4 | 10 |
| β-strand | 443-446 | 4 | 10 |
| β-strand | 452 | 1 | 10 |
| α-helix | 455-460 | 6 | |
| β-strand | 463 | 1 | 9 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| α-helix | 502-517 | 16 | |
| β-strand | 522-527 | 6 | 13 |
| β-strand | 534-539 | 6 | 13 |
| β-strand | 550 | 1 | 14 |
| β-strand | 551-556 | 6 | 13 |
| α-helix | 565-566 | 2 | |
| β-strand | 567-570 | 4 | 13 |
| α-helix | 601-613 | 13 | |
| α-helix | 623-631 | 9 | |
| α-helix | 633-647 | 15 | |
| β-strand | 649 | 1 | 14 |
| α-helix | 650-651 | 2 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| β-strand | 702-706 | 5 | 11 |
| β-strand | 713-716 | 4 | 11 |
| β-strand | 722 | 1 | 12 |
| α-helix | 723-733 | 11 | |
| α-helix | 738-740 | 3 | |
| β-strand | 741-744 | 4 | 11 |
| β-strand | 749 | 1 | 11 |
| α-helix | 750-751 | 2 | |
| β-strand | 755 | 1 | 12 |
| α-helix | 756-759 | 4 | |
| β-strand | 766-771 | 6 | 11 |
| α-helix | 772 | 1 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| E3 ubiquitin-protein ligase parkin | B | protein | 322 | Homo sapiens | O60260 (AlphaFold model) |
| ubiquitin | D | protein | 76 | Homo sapiens | P0CG47 (AlphaFold model) |
| Ubiquitin-conjugating enzyme E2 L3 | C | protein | 156 | Homo sapiens | P68036 (AlphaFold model) |
| phosphoubiquitin | A | protein | 76 | Homo sapiens | P0CG48 (AlphaFold model) |
>6N13_1 E3 ubiquitin-protein ligase parkin (chains B) NSFYVYCKGPCQRVQPGKLRVQCSTCRQATLTLTQGPSCWDDVLIPNRMSGECQSPHCPG TSAEFFFKCGAHPTSDKETSVALHLIATNSRNITCITCTDVRSPVLVFQCNSRHVICLDC FHLYCVTRLNDRQFVHDPQLGYSLPCVAGCPNSLIKELHHFRILGEEQYNRYQQYGAEEC VLQMGGVLCPRPGCGAGLLPEPDCRKVTCEGGNGLGCGFAFCRECKEAYHEGECSAVFEA SGTTTQAYRVDERAAEQARWEAASKETIKKTTKPCPRCHVPVEKNGGCMHMKCPQPQCRL EWCWNCGCEWNRVCMGDHWFDV
>6N13_2 ubiquitin (chains D) MQIFVKTLTGKTITLEVEPSDTIENVKAKIQDKEGIPPDQQRLIFAGKQLEDGRTLSDYN IQKESTLHLVLRLRGG
>6N13_3 Ubiquitin-conjugating enzyme E2 L3 (chains C) GHMAASRRLMKELEEIRKSGMKNFRNIQVDEANLLTWQGLIVPDNPPYDKGAFRIEINFP AEYPFKPPKITFKTKIYHPNIDEKGQVKLPVISAENWKPATKTDQVIQSLIALVNDPQPE HPLRADLAEEYSKDRKKFSKNAEEFTKKYGEKRPVD
>6N13_4 phosphoubiquitin (chains A) MQIFVKTLTGKTITLEVEPSDTIENVKAKIQDKEGIPPDQQRLIFAGKQLEDGRTLSDYN IQKESTLHLVLRLRGG
| ID | Name | Formula | Copies |
|---|---|---|---|
| ZN | Zinc ion | Zn | 8 |
Synergistic recruitment of UbcH7~Ub and phosphorylated Ubl domain triggers parkin activation. Condos, T.E., Dunkerley, K.M., Freeman, E.A. et al. EMBO J (2018) 37. DOI 10.15252/embj.2018100014 · 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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