Atg8 transfer from Atg7 to Atg3: a distinctive E1-E2 architecture and mechanism in the autophagy pathway. Determined by X-ray diffraction at 1.6 Å resolution. Released 23 Nov 2011.
Explore 3T7H in 3D Show helices and sheets RCSB PDB PDBe
3T7H contains 20 α-helices and 38 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 |
|---|---|---|---|
| β-strand | 5-6 | 2 | 1 |
| β-strand | 10 | 1 | 2 |
| β-strand | 13-17 | 5 | 3 |
| α-helix | 19-29 | 11 | |
| β-strand | 37-46 | 10 | 4 |
| β-strand | 57 | 1 | 5 |
| β-strand | 58-62 | 5 | 3 |
| α-helix | 64-67 | 4 | |
| β-strand | 78-87 | 10 | 4 |
| α-helix | 90-95 | 6 | |
| α-helix | 98-113 | 16 | |
| α-helix | 117-119 | 3 | |
| β-strand | 123-130 | 8 | 4 |
| β-strand | 135-146 | 12 | 4 |
| β-strand | 151-157 | 7 | 1 |
| α-helix | 159-164 | 6 | |
| α-helix | 165-174 | 10 | |
| β-strand | 180-183 | 4 | 1 |
| β-strand | 189-191 | 3 | 1 |
| α-helix | 194-200 | 7 | |
| β-strand | 202-206 | 5 | 1 |
| β-strand | 209 | 1 | 5 |
| β-strand | 216 | 1 | 2 |
| α-helix | 219-229 | 11 | |
| β-strand | 235-241 | 7 | 1 |
| β-strand | 248-256 | 9 | 1 |
| β-strand | 269-273 | 5 | 4 |
| α-helix | 274-275 | 2 | |
| β-strand | 284-287 | 4 | 4 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| Ubiquitin-like modifier-activating enzyme ATG7 | A, B | protein | 291 | Saccharomyces cerevisiae | P38862 (AlphaFold model) |
>3T7H_1 Ubiquitin-like modifier-activating enzyme ATG7 (chains A, B) GSMSSERVLSYAPAFKSFLDTSFFQELSRLKLDVLKLDSTCQPLTVNLDLHNIPKSADQV PLFLTNRSFEKHNNKRTNEVPLQGSIFNFNVLDEFKNLDKQLFLHQRALECWEDGIKDIN KCVSFVIISFADLKKYRFYYWLGVPCFQRPSSTVLHVRPEPSLKGLFSKCQKWFDVNYSK WVCILDADDEIVNYDKCIIRKTKVLAIRDTSTMENVPSALTKNFLSVLQYDVPDLIDFKL LIIRQNEGSFALNATFASIDPQSSSSNPDMKVSGWERNVQGKLADRVVDLS
Atg8 transfer from atg7 to atg3: a distinctive e1-e2 architecture and mechanism in the autophagy pathway. Taherbhoy, A.M., Tait, S.W., Kaiser, S.E. et al. Mol Cell (2011) 44:451-461. DOI 10.1016/j.molcel.2011.08.034 · 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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