Crystal structure ATG9 HDIR in complex with the ATG13:ATG101 HORMA dimer. Determined by X-ray diffraction at 2.41 Å resolution. Released 23 Nov 2022.
Explore 8DO8 in 3D Show helices and sheets RCSB PDB PDBe
8DO8 contains 32 α-helices and 50 β-strands across 6 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 | 4-12 | 9 | 1 |
| α-helix | 14-16 | 3 | |
| α-helix | 17-31 | 15 | |
| β-strand | 33-34 | 2 | 2 |
| α-helix | 35-36 | 2 | |
| β-strand | 37-41 | 5 | 3 |
| β-strand | 44-47 | 4 | 3 |
| β-strand | 49 | 1 | 4 |
| β-strand | 50 | 1 | 5 |
| β-strand | 52-56 | 5 | 6 |
| β-strand | 63-67 | 5 | 6 |
| α-helix | 70-86 | 17 | |
| β-strand | 97-106 | 10 | 1 |
| α-helix | 107-109 | 3 | |
| α-helix | 113-114 | 2 | |
| β-strand | 115-128 | 14 | 1 |
| α-helix | 140-160 | 21 | |
| α-helix | 166-170 | 5 | |
| α-helix | 174-176 | 3 | |
| β-strand | 178 | 1 | 7 |
| β-strand | 186-187 | 2 | 2 |
| β-strand | 188 | 1 | 7 |
| α-helix | 189 | 1 | |
| β-strand | 190-194 | 5 | 1 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| α-helix | 7-30 | 24 | |
| β-strand | 38 | 1 | 6 |
| β-strand | 42 | 1 | 4 |
| α-helix | 50-52 | 3 | |
| β-strand | 53 | 1 | 5 |
| α-helix | 59-69 | 11 | |
| β-strand | 75 | 1 | 8 |
| β-strand | 78 | 1 | 8 |
| β-strand | 79-88 | 10 | 9 |
| β-strand | 93-104 | 12 | 9 |
| α-helix | 113-117 | 5 | |
| α-helix | 118-132 | 15 | |
| α-helix | 136-142 | 7 | |
| β-strand | 148-157 | 10 | 9 |
| β-strand | 169-177 | 9 | 9 |
| β-strand | 182-189 | 8 | 9 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| β-strand | 4-12 | 9 | 10 |
| α-helix | 14-16 | 3 | |
| α-helix | 17-31 | 15 | |
| β-strand | 33-34 | 2 | 11 |
| α-helix | 35-36 | 2 | |
| β-strand | 37-39 | 3 | 12 |
| β-strand | 44-47 | 4 | 12 |
| β-strand | 49 | 1 | 13 |
| β-strand | 50 | 1 | 14 |
| β-strand | 52-56 | 5 | 15 |
| β-strand | 63-67 | 5 | 15 |
| α-helix | 70-90 | 21 | |
| β-strand | 95-106 | 12 | 10 |
| α-helix | 113-114 | 2 | |
| β-strand | 115-128 | 14 | 10 |
| α-helix | 137-159 | 23 | |
| α-helix | 166-170 | 5 | |
| α-helix | 174-176 | 3 | |
| β-strand | 178 | 1 | 16 |
| β-strand | 186-187 | 2 | 11 |
| β-strand | 188 | 1 | 16 |
| α-helix | 189 | 1 | |
| β-strand | 190-196 | 7 | 10 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| α-helix | 7-30 | 24 | |
| β-strand | 38 | 1 | 15 |
| β-strand | 42 | 1 | 13 |
| α-helix | 50-52 | 3 | |
| β-strand | 53 | 1 | 14 |
| α-helix | 56-58 | 3 | |
| α-helix | 59-69 | 11 | |
| β-strand | 75 | 1 | 17 |
| β-strand | 78 | 1 | 17 |
| β-strand | 79-88 | 10 | 18 |
| β-strand | 93-103 | 11 | 18 |
| α-helix | 113-117 | 5 | |
| α-helix | 118-132 | 15 | |
| α-helix | 136-142 | 7 | |
| β-strand | 148-157 | 10 | 18 |
| β-strand | 169-178 | 10 | 18 |
| β-strand | 181-189 | 9 | 18 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| β-strand | 837-838 | 2 | 3 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| Autophagy-related protein 101 | A, C, E, F | protein | 218 | Homo sapiens | Q9BSB4 (AlphaFold model) |
| Autophagy-related protein 13 | B, D | protein | 197 | Homo sapiens | O75143 (AlphaFold model) |
>8DO8_1 Autophagy-related protein 101 (chains A, C, E, F) GGTSEDELPPQVHKVGSDEAMNCRSEVLEVSVEGRQVEEAMLAVLHTVLLHRSTGKFHYK KEGTYSIGTVGTQDVDCDFIDFTYVRVSSEELDRALRKVVGEFKDALRNSGGDGLGQMSL EFYQKKKSRWPFSDECIPWEVWTVKVHVVALATEQERQICREKVGEKLCEKIINIVEVMN RHEYLPKMPTQSEVDNVFDTGLRDVQPYLYKISFQITD
>8DO8_2 Autophagy-related protein 13 (chains B, D) METDLNSQDRKDLDKFIKFFALKTVQVIVQARLGEKICTRSSSSPTGSDWFNLAIKDIPE VTHEAKKALAGQLPAVGRSMCVEISLKTSEGDSMELEIWCLEMNEKCDKEIKVSYTVYNR LSLLLKSLLAITRVTPAYRLSRKQGHEYVILYRIYFGEVQLSGLGEGFQTVRVGTVGTPV GTITLSCAYRINLAFMS
Structural basis for ATG9A recruitment to the ULK1 complex in mitophagy initiation. Ren, X., Nguyen, T.N., Lam, W.K. et al. Sci Adv (2023) 9:eadg2997-eadg2997. DOI 10.1126/sciadv.adg2997 · PubMed
Other PDB entries of the same protein (UniProt Q9BSB4 (AlphaFold model), which also has an AlphaFold model), best resolution first:
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