HOIP-HOIPIN1 complex. Determined by X-ray diffraction at 1.54 Å resolution. Released 15 Apr 2020.
Explore 6KC5 in 3D Show helices and sheets RCSB PDB PDBe
6KC5 contains 12 α-helices and 7 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 | 870 | 1 | 1 |
| β-strand | 877 | 1 | 1 |
| β-strand | 887-889 | 3 | 2 |
| β-strand | 896-898 | 3 | 2 |
| α-helix | 903 | 1 | |
| β-strand | 904 | 1 | 2 |
| β-strand | 905-906 | 2 | 3 |
| β-strand | 923-924 | 2 | 3 |
| α-helix | 931-934 | 4 | |
| α-helix | 939-948 | 10 | |
| α-helix | 957-959 | 3 | |
| α-helix | 999-1012 | 14 | |
| α-helix | 1017-1020 | 4 | |
| α-helix | 1023-1029 | 7 | |
| α-helix | 1030-1034 | 5 | |
| α-helix | 1040-1041 | 2 | |
| α-helix | 1046-1060 | 15 | |
| α-helix | 1062 | 1 | |
| α-helix | 1064 | 1 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| E3 ubiquitin-protein ligase RNF31 | B | protein | 225 | Homo sapiens | Q96EP0 (AlphaFold model) |
>6KC5_1 E3 ubiquitin-protein ligase RNF31 (chains B) GPGHMPEYQAQGLAMYLQENGIDCPKCKFSYALARGGCMHFHCTQCRHQFCSGCYNAFYA KNKCPEPNCRVKKSLHGHHPRDCLFYLRDWTALRLQKLLQDNNVMFNTEPPAGARAVPGG GCRVIEQKEVPNGLRDEACGKETPAGYAGLCQAHYKEYLVSLINAHSLDPATLYEVEELE TATERYLHVRPQPLAGEDPPAYQARLLQKLTEEVPLGQSIPRRRK
| ID | Name | Formula | Copies |
|---|---|---|---|
| ZN | Zinc ion | Zn | 4 |
| D5U | 2-[3-(2-methoxyphenyl)-3-oxidanylidene-propyl]benzoic acid | C17 H16 O4 | 1 |
Water and common crystallization additives (GOL, EPE) are not listed.
Molecular bases for HOIPINs-mediated inhibition of LUBAC and innate immune responses. Oikawa, D., Sato, Y., Ohtake, F. et al. Commun Biol (2020) 3:163-163. DOI 10.1038/s42003-020-0882-8 · PubMed
Other PDB entries of the same protein (UniProt Q96EP0 (AlphaFold model), which also has an AlphaFold model), best resolution first:
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