Crystal structure of Atg7C-Atg8 complex. Determined by X-ray diffraction at 1.91 Å resolution. Released 23 Nov 2011.
Explore 3RUI in 3D Show helices and sheets RCSB PDB PDBe
3RUI contains 25 α-helices and 23 β-strands across 2 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 | 294-308 | 15 | |
| α-helix | 309-313 | 5 | |
| α-helix | 319-323 | 5 | |
| β-strand | 326-330 | 5 | 1 |
| α-helix | 334-345 | 12 | |
| β-strand | 350-354 | 5 | 1 |
| β-strand | 358 | 1 | 2 |
| α-helix | 372-374 | 3 | |
| β-strand | 378 | 1 | 2 |
| α-helix | 379-390 | 12 | |
| β-strand | 395-399 | 5 | 1 |
| α-helix | 402-404 | 3 | |
| α-helix | 413-429 | 17 | |
| β-strand | 432-435 | 4 | 1 |
| α-helix | 441-443 | 3 | |
| α-helix | 444-452 | 9 | |
| β-strand | 456-462 | 7 | 1 |
| β-strand | 466-471 | 6 | 1 |
| β-strand | 483 | 1 | 3 |
| α-helix | 486-489 | 4 | |
| α-helix | 504-508 | 5 | |
| α-helix | 512-529 | 18 | |
| α-helix | 532-534 | 3 | |
| β-strand | 539-540 | 2 | 4 |
| β-strand | 543-544 | 2 | 4 |
| β-strand | 548-552 | 5 | 1 |
| β-strand | 557-561 | 5 | 1 |
| β-strand | 564 | 1 | 3 |
| α-helix | 565-566 | 2 | |
| α-helix | 574-583 | 10 | |
| α-helix | 585-593 | 9 | |
| α-helix | 595-602 | 8 | |
| α-helix | 604-612 | 9 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| α-helix | 11-24 | 14 | |
| β-strand | 28-35 | 8 | 5 |
| α-helix | 36 | 1 | |
| β-strand | 48-52 | 5 | 5 |
| β-strand | 56 | 1 | 6 |
| α-helix | 57-67 | 11 | |
| β-strand | 76-79 | 4 | 5 |
| β-strand | 80 | 1 | 7 |
| β-strand | 83 | 1 | 7 |
| β-strand | 90 | 1 | 6 |
| α-helix | 91-98 | 8 | |
| α-helix | 104 | 1 | |
| β-strand | 105-111 | 7 | 5 |
| α-helix | 112-113 | 2 | |
| β-strand | 115 | 1 | 1 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| Ubiquitin-like modifier-activating enzyme ATG7 | A | protein | 340 | Saccharomyces cerevisiae | P38862 (AlphaFold model) |
| Autophagy-related protein 8 | B | protein | 118 | Saccharomyces cerevisiae | P38182 (AlphaFold model) |
>3RUI_1 Ubiquitin-like modifier-activating enzyme ATG7 (chains A) GSDPLKIADQSVDLNLKLMKWRILPDLNLDIIKNTKVLLLGAGTLGCYVSRALIAWGVRK ITFVDNGTVSYSNPVRQALYNFEDCGKPKAELAAASLKRIFPLMDATGVKLSIPMIGHKL VNEEAQHKDFDRLRALIKEHDIIFLLVDSRESRWLPSLLSNIENKTVINAALGFDSYLVM RHGNRDEQSSKQLGCYFCHDVVAPTDSLTDRTLDQMSTVTRPGVAMMASSLAVELMTSLL QTKYSGSETTVLGDIPHQIRGFLHNFSILKLETPAYEHCPACSPKVIEAFTDLGWEFVKK ALEHPLYLEEISGLSVIKQEVERLGNDVFEWEDDESDEIA
>3RUI_2 Autophagy-related protein 8 (chains B) GSMKSTFKSEYPFEKRKAESERIADRFKNRIPVICEKAEKSDIPEIDKRKYLVPADLTVG QFVYVIRKRIMLPPEKAIFIFVNDTLPPTAALMSAIYQEHKDKDGFLYVTYSGENTFG
| ID | Name | Formula | Copies |
|---|---|---|---|
| ZN | Zinc ion | Zn | 1 |
Insights into noncanonical E1 enzyme activation from the structure of autophagic E1 Atg7 with Atg8. Hong, S.B., Kim, B.W., Lee, K.E. et al. Nat Struct Mol Biol (2011) 18:1323-1330. DOI 10.1038/nsmb.2165 · PubMed
Other PDB entries of the same protein (UniProt P38862 (AlphaFold model), which also has an AlphaFold model), best resolution first:
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