Crystal structure of WIPI3 in complex with ATG16L1. Determined by X-ray diffraction at 2.77 Å resolution. Released 1 Jan 2025.
Explore 8ZQG in 3D Show helices and sheets RCSB PDB PDBe
8ZQG contains 6 α-helices and 59 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 | 13-18 | 6 | 8 |
| β-strand | 24-29 | 6 | 8 |
| β-strand | 32-37 | 6 | 8 |
| β-strand | 42-48 | 7 | 8 |
| β-strand | 53-59 | 7 | 9 |
| β-strand | 65-71 | 7 | 9 |
| β-strand | 75 | 1 | 9 |
| β-strand | 81-86 | 6 | 9 |
| β-strand | 91-97 | 7 | 9 |
| β-strand | 102-107 | 6 | 10 |
| β-strand | 111-116 | 6 | 10 |
| β-strand | 119-124 | 6 | 10 |
| β-strand | 131-136 | 6 | 10 |
| β-strand | 146-147 | 2 | 11 |
| β-strand | 155-159 | 5 | 11 |
| β-strand | 165-170 | 6 | 11 |
| α-helix | 177-178 | 2 | |
| β-strand | 179-182 | 4 | 11 |
| β-strand | 188-193 | 6 | 12 |
| β-strand | 199-204 | 6 | 12 |
| β-strand | 209-214 | 6 | 12 |
| β-strand | 220-225 | 6 | 12 |
| β-strand | 233-238 | 6 | 13 |
| β-strand | 244-249 | 6 | 13 |
| α-helix | 250-252 | 3 | |
| β-strand | 253-258 | 6 | 13 |
| β-strand | 287-290 | 4 | 13 |
| β-strand | 297-301 | 5 | 14 |
| β-strand | 307-312 | 6 | 14 |
| β-strand | 316-322 | 7 | 14 |
| β-strand | 328-335 | 8 | 14 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| β-strand | 13-18 | 6 | 1 |
| β-strand | 24-29 | 6 | 1 |
| β-strand | 32-37 | 6 | 1 |
| β-strand | 42-48 | 7 | 1 |
| β-strand | 53-59 | 7 | 2 |
| β-strand | 65-71 | 7 | 2 |
| β-strand | 75 | 1 | 2 |
| β-strand | 81-86 | 6 | 2 |
| β-strand | 91-97 | 7 | 2 |
| β-strand | 102-107 | 6 | 3 |
| β-strand | 111-116 | 6 | 3 |
| β-strand | 119-124 | 6 | 3 |
| β-strand | 131-136 | 6 | 3 |
| β-strand | 146-147 | 2 | 4 |
| β-strand | 155-159 | 5 | 4 |
| β-strand | 165-170 | 6 | 4 |
| α-helix | 177-178 | 2 | |
| β-strand | 179-182 | 4 | 4 |
| β-strand | 188-193 | 6 | 5 |
| β-strand | 199-204 | 6 | 5 |
| β-strand | 209-214 | 6 | 5 |
| β-strand | 220-225 | 6 | 5 |
| β-strand | 233-238 | 6 | 6 |
| β-strand | 244-249 | 6 | 6 |
| α-helix | 250-252 | 3 | |
| β-strand | 253-258 | 6 | 6 |
| β-strand | 284 | 1 | 5 |
| β-strand | 287-290 | 4 | 6 |
| β-strand | 297-301 | 5 | 7 |
| β-strand | 307-312 | 6 | 7 |
| β-strand | 316-322 | 7 | 7 |
| β-strand | 328-335 | 8 | 7 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| α-helix | 127-175 | 49 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| α-helix | 127-176 | 50 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| WD repeat domain phosphoinositide-interacting protein 3 | A, B | protein | 323 | Homo sapiens | Q5MNZ6 (AlphaFold model) |
| Autophagy-related protein 16-1 | C, D | protein | 69 | Homo sapiens | Q676U5 (AlphaFold model) |
>8ZQG_1 WD repeat domain phosphoinositide-interacting protein 3 (chains A, B) GPGSPHGNGLLYAGFNQDHGCFACGMENGFRVYNTDPLKEKEKQEFLEGGVGHVEMLFRC NYLALVGGGKKPKYPPNKVMIWDDLKKKTVIEIEFSTEVKAVKLRRDRIVVVLDSMIKVF TFTHNPHQLHVFETCYNPKGLCVLCPNSNNSLLAFPGTHTGHVQLVDLASTEKPPVDIPA HEGVLSCIALNLQGTRIATASEKGTLIRIFDTSSGHLIQELRRGSQAANIYCINFNQDAS LICVSSDHGTVHIFAAEDPKSKWSFSKFQVPSGSPCICAFGTEPNAVIAICADGSYYKFL FNPKGECIRDVYAQFLEMTDDKL
>8ZQG_2 Autophagy-related protein 16-1 (chains C, D) GPGSMQMNEAKIAECLQTISDLETECLDLRTKLCDLERANQTLKDEYDALQITFTALEGK LRKTTEENQ
Structure of the WIPI3/ATG16L1 Complex Reveals the Molecular Basis for the Recruitment of the ATG12~ATG5-ATG16L1 Complex by WIPI3. Gong, X., Wang, Y., Zhou, Y. et al. Cells (2024) 13. DOI 10.3390/cells13242113 · PubMed
Other PDB entries of the same protein (UniProt Q5MNZ6 (AlphaFold model), which also has an AlphaFold model), best resolution first:
MolViewer shows 8ZQG directly in your browser with nothing to install. Switch between cartoon, ball-and-stick, spacefill and surface views, color by chain, secondary structure or B-factor, measure distances, angles and dihedrals, and share or embed the view.