Crystal structure of ATG101-ATG13HORMA. Determined by X-ray diffraction at 2.51 Å resolution. Released 4 Jul 2018.
Explore 5XV1 in 3D Show helices and sheets RCSB PDB PDBe
5XV1 contains 33 α-helices and 48 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 |
|---|---|---|---|
| α-helix | 8-30 | 23 | |
| β-strand | 38 | 1 | 1 |
| β-strand | 42 | 1 | 2 |
| α-helix | 50-52 | 3 | |
| β-strand | 53 | 1 | 3 |
| α-helix | 56-58 | 3 | |
| α-helix | 59-69 | 11 | |
| β-strand | 75 | 1 | 4 |
| β-strand | 78 | 1 | 4 |
| β-strand | 79-88 | 10 | 5 |
| β-strand | 93-103 | 11 | 5 |
| α-helix | 115-131 | 17 | |
| α-helix | 136-142 | 7 | |
| β-strand | 148-157 | 10 | 5 |
| α-helix | 162-164 | 3 | |
| β-strand | 169-178 | 10 | 5 |
| β-strand | 181-189 | 9 | 5 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| β-strand | 4-12 | 9 | 6 |
| α-helix | 14-16 | 3 | |
| α-helix | 17-31 | 15 | |
| β-strand | 33-34 | 2 | 7 |
| α-helix | 35-36 | 2 | |
| β-strand | 37-39 | 3 | 8 |
| β-strand | 45-47 | 3 | 8 |
| β-strand | 49 | 1 | 2 |
| β-strand | 50 | 1 | 3 |
| α-helix | 51 | 1 | |
| β-strand | 52-56 | 5 | 1 |
| β-strand | 63-67 | 5 | 1 |
| α-helix | 70-90 | 21 | |
| β-strand | 95-106 | 12 | 6 |
| α-helix | 113-114 | 2 | |
| β-strand | 115-128 | 14 | 6 |
| α-helix | 134-161 | 28 | |
| α-helix | 166-169 | 4 | |
| α-helix | 174-176 | 3 | |
| β-strand | 178 | 1 | 9 |
| β-strand | 186-187 | 2 | 7 |
| β-strand | 188 | 1 | 9 |
| β-strand | 190-196 | 7 | 6 |
| α-helix | 205-210 | 6 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| α-helix | 8-31 | 24 | |
| β-strand | 38 | 1 | 10 |
| β-strand | 42 | 1 | 11 |
| α-helix | 50-52 | 3 | |
| β-strand | 53 | 1 | 12 |
| α-helix | 59-69 | 11 | |
| β-strand | 75 | 1 | 13 |
| β-strand | 78 | 1 | 13 |
| β-strand | 79-88 | 10 | 14 |
| β-strand | 93-103 | 11 | 14 |
| α-helix | 116-131 | 16 | |
| α-helix | 136-141 | 6 | |
| β-strand | 148-157 | 10 | 14 |
| α-helix | 162-164 | 3 | |
| β-strand | 169-178 | 10 | 14 |
| β-strand | 181-189 | 9 | 14 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| β-strand | 4-13 | 10 | 15 |
| α-helix | 14-16 | 3 | |
| α-helix | 17-31 | 15 | |
| β-strand | 33-34 | 2 | 16 |
| α-helix | 35-36 | 2 | |
| β-strand | 37-39 | 3 | 17 |
| β-strand | 45-47 | 3 | 17 |
| β-strand | 49 | 1 | 11 |
| β-strand | 50 | 1 | 12 |
| α-helix | 51 | 1 | |
| β-strand | 52-56 | 5 | 10 |
| β-strand | 63-67 | 5 | 10 |
| α-helix | 70-88 | 19 | |
| β-strand | 95-106 | 12 | 15 |
| α-helix | 113-114 | 2 | |
| β-strand | 115-129 | 15 | 15 |
| α-helix | 135-159 | 25 | |
| α-helix | 166-169 | 4 | |
| α-helix | 173-176 | 4 | |
| β-strand | 178 | 1 | 18 |
| β-strand | 186-187 | 2 | 16 |
| β-strand | 188 | 1 | 18 |
| β-strand | 190-196 | 7 | 15 |
| α-helix | 206-215 | 10 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| Autophagy-related protein 13 | A, C | protein | 190 | Homo sapiens | O75143 (AlphaFold model) |
| Autophagy-related protein 101 | B, D | protein | 218 | Homo sapiens | Q9BSB4 (AlphaFold model) |
>5XV1_1 Autophagy-related protein 13 (chains A, C) METDLNSQDRKDLDKFIKFFALKTVQVIVQARLGEKICTRSSSSPTGSDWFNLAIKDIPE VTHEAKKALAGQLPAVGRSMCVEISLKTSEGDSMELEIWCLEMNEKCDKEIKVSYTVYNR LSLLLKSLLAITRVTPAYRLSRKQGHEYVILYRIYFGEVQLSGLGEGFQTVRVGTVGTPV GTITLSCAYR
>5XV1_2 Autophagy-related protein 101 (chains B, D) MNCRSEVLEVSVEGRQVEEAMLAVLHTVLLHRSTGKFHYAAAGTYSIGTVGTQDVDCDFI DFTYVRVSSEELDRALRKVVGEFKDALRNSGGDGLGQMSLEFYQKKKSRWPFSDECIPWE VWTVKVHVVALATEQERQICREKVGEKLCEKIINIVEVMNRHEYLPKMPTQSEVDNVFDT GLRDVQPYLYKISFQITDALGTSVTTTMRRLIKDTLAL
Crystal structure of ATG101-ATG13HORMA. Kim, B.-W., Song, H.K. To be published.
Other PDB entries of the same protein (UniProt O75143 (AlphaFold model), which also has an AlphaFold model), best resolution first:
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