Crystal structure of an Atg7-Atg10 crosslinked complex. Determined by X-ray diffraction at 2.9 Å resolution. Released 14 Nov 2012.
Explore 4GSK in 3D Show helices and sheets RCSB PDB PDBe
4GSK contains 62 α-helices and 78 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 | 5-6 | 2 | 1 |
| β-strand | 10 | 1 | 2 |
| β-strand | 14-17 | 4 | 3 |
| α-helix | 19-29 | 11 | |
| β-strand | 39-46 | 8 | 4 |
| β-strand | 57 | 1 | 5 |
| β-strand | 59-62 | 4 | 3 |
| α-helix | 64-66 | 3 | |
| β-strand | 78-87 | 10 | 4 |
| α-helix | 90-95 | 6 | |
| α-helix | 98-115 | 18 | |
| α-helix | 117-119 | 3 | |
| β-strand | 123-130 | 8 | 4 |
| β-strand | 135-146 | 12 | 4 |
| β-strand | 152-157 | 6 | 1 |
| α-helix | 159-164 | 6 | |
| α-helix | 165-174 | 10 | |
| β-strand | 180-183 | 4 | 1 |
| β-strand | 189-190 | 2 | 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 | 248-255 | 8 | 1 |
| β-strand | 269-273 | 5 | 4 |
| α-helix | 274 | 1 | |
| β-strand | 275 | 1 | 6 |
| β-strand | 281 | 1 | 6 |
| β-strand | 284-287 | 4 | 4 |
| α-helix | 294-308 | 15 | |
| α-helix | 309-313 | 5 | |
| α-helix | 320-323 | 4 | |
| β-strand | 326-330 | 5 | 7 |
| α-helix | 334-345 | 12 | |
| β-strand | 350-355 | 6 | 7 |
| β-strand | 358 | 1 | 8 |
| α-helix | 363-365 | 3 | |
| α-helix | 372-374 | 3 | |
| β-strand | 378 | 1 | 8 |
| α-helix | 379-390 | 12 | |
| β-strand | 395-400 | 6 | 7 |
| α-helix | 404-405 | 2 | |
| α-helix | 413-428 | 16 | |
| β-strand | 432-435 | 4 | 7 |
| α-helix | 444-452 | 9 | |
| β-strand | 456-462 | 7 | 7 |
| β-strand | 466-471 | 6 | 7 |
| α-helix | 486-488 | 3 | |
| α-helix | 512-529 | 18 | |
| α-helix | 532-534 | 3 | |
| β-strand | 540 | 1 | 9 |
| β-strand | 543 | 1 | 9 |
| β-strand | 548-552 | 5 | 7 |
| β-strand | 557-561 | 5 | 7 |
| α-helix | 574-583 | 10 | |
| α-helix | 585-593 | 9 | |
| α-helix | 595-602 | 8 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| β-strand | 5-6 | 2 | 10 |
| β-strand | 10 | 1 | 11 |
| β-strand | 14-17 | 4 | 12 |
| α-helix | 19-29 | 11 | |
| β-strand | 40-46 | 7 | 13 |
| β-strand | 57 | 1 | 14 |
| β-strand | 59-62 | 4 | 12 |
| α-helix | 64-67 | 4 | |
| β-strand | 78-87 | 10 | 13 |
| α-helix | 90-95 | 6 | |
| α-helix | 98-115 | 18 | |
| α-helix | 117-119 | 3 | |
| β-strand | 123-130 | 8 | 13 |
| β-strand | 135-146 | 12 | 13 |
| β-strand | 151-157 | 7 | 10 |
| α-helix | 159-164 | 6 | |
| α-helix | 165-174 | 10 | |
| β-strand | 180-183 | 4 | 10 |
| β-strand | 189-191 | 3 | 10 |
| α-helix | 194-200 | 7 | |
| β-strand | 202-206 | 5 | 10 |
| β-strand | 209 | 1 | 14 |
| β-strand | 216 | 1 | 11 |
| α-helix | 219-229 | 11 | |
| β-strand | 235-241 | 7 | 10 |
| β-strand | 248-256 | 9 | 10 |
| β-strand | 269-273 | 5 | 13 |
| α-helix | 274-275 | 2 | |
| β-strand | 284-287 | 4 | 13 |
| α-helix | 289-292 | 4 | |
| α-helix | 294-308 | 15 | |
| α-helix | 309-313 | 5 | |
| α-helix | 320-324 | 5 | |
| β-strand | 326-330 | 5 | 15 |
| α-helix | 334-345 | 12 | |
| β-strand | 350-354 | 5 | 15 |
| β-strand | 358 | 1 | 16 |
| α-helix | 363-366 | 4 | |
| α-helix | 372-374 | 3 | |
| β-strand | 378 | 1 | 16 |
| α-helix | 379-390 | 12 | |
| β-strand | 395-399 | 5 | 15 |
| α-helix | 404-405 | 2 | |
| α-helix | 413-429 | 17 | |
| β-strand | 432-435 | 4 | 15 |
| β-strand | 439 | 1 | 17 |
| α-helix | 440-452 | 13 | |
| β-strand | 456-462 | 7 | 15 |
| β-strand | 466-472 | 7 | 15 |
| β-strand | 505 | 1 | 17 |
| α-helix | 512-529 | 18 | |
| β-strand | 539-540 | 2 | 18 |
| β-strand | 543-544 | 2 | 18 |
| β-strand | 548-552 | 5 | 15 |
| β-strand | 557-561 | 5 | 15 |
| α-helix | 564-566 | 3 | |
| α-helix | 574-583 | 10 | |
| α-helix | 585-593 | 9 | |
| α-helix | 595-602 | 8 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| α-helix | 4-16 | 13 | |
| β-strand | 26-31 | 6 | 13 |
| β-strand | 38-42 | 5 | 13 |
| α-helix | 43-45 | 3 | |
| α-helix | 46-54 | 9 | |
| β-strand | 59-70 | 12 | 13 |
| β-strand | 75-87 | 13 | 13 |
| β-strand | 92-97 | 6 | 13 |
| β-strand | 128-129 | 2 | 13 |
| α-helix | 149-157 | 9 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| α-helix | 4-16 | 13 | |
| β-strand | 26-31 | 6 | 4 |
| β-strand | 38-42 | 5 | 4 |
| α-helix | 43-45 | 3 | |
| α-helix | 46-55 | 10 | |
| β-strand | 59-70 | 12 | 4 |
| β-strand | 75-87 | 13 | 4 |
| β-strand | 92-97 | 6 | 4 |
| β-strand | 128-129 | 2 | 4 |
| α-helix | 149-154 | 6 | |
| α-helix | 155-159 | 5 | |
| α-helix | 160-162 | 3 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| Ubiquitin-like modifier-activating enzyme ATG7 | A, B | protein | 615 | Saccharomyces cerevisiae | P38862 (AlphaFold model) |
| Ubiquitin-like-conjugating enzyme ATG10 | Y, Z | protein | 173 | Saccharomyces cerevisiae | Q07879 (AlphaFold model) |
>4GSK_1 Ubiquitin-like modifier-activating enzyme ATG7 (chains A, B) GSMSSERVLSYAPAFKSFLDTSFFQELSRLKLDVLKLDSTSQPLTVNLDLHNIPKSADQV PLFLTNRSFEKHNNKRTNEVPLQGSIFNFNVLDEFKNLDKQLFLHQRALECWEDGIKDIN KCVSFVIISFADLKKYRFYYWLGVPCFQRPSSTVLHVRPEPSLKGLFSKCQKWFDVNYSK WVCILDADDEIVNYDKSIIRKTKVLAIRDTSTMENVPSALTKNFLSVLQYDVPDLIDFKL LIIRQNEGSFALNATFASIDPQSSSSNPDMKVSGWERNVQGKLAPRVVDLSSLLDPLKIA DQSVDLNLKLMKWRILPDLNLDIIKNTKVLLLGAGTLGCYVSRALIAWGVRKITFVDNGT VSYSNPVRQALYNFEDAGKPKAELAAASLKRIFPLMDATGVKLSIPMIGHKLVNEEAQHK DFDRLRALIKEHDIIFLLVDSRESRWLPSLLSNIENKTVINAALGFDSYLVMRHGNRDEQ SSKQLGCYFCHDVVAPTDSLTDRTLDQMCTVTRPGVAMMASSLAVELMTSLLQTKYSGSE TTVLGDIPHQIRGFLHNFSILKLETPAYEHCPACSPKVIEAFTDLGWEFVKKALEHPLYL EEISGLSVIKQEVER
>4GSK_2 Ubiquitin-like-conjugating enzyme ATG10 (chains Y, Z) GSGGSGMIPYQEWHSQLQSLYDSQIFHNWALSQDVHLNDEKDGLLLRLIPTRQLQKNTER IENKLLNHIELYLTYSKVYNEPLLLLRIWEEKSIDGIPMTKLMLPTDIESLLDVQGKFQL GLDTIINLEGSVWYSFHPCDTSSIVGDQAEFMSTYLRRWVSIFIFSWLGYEDS
| ID | Name | Formula | Copies |
|---|---|---|---|
| ZN | Zinc ion | Zn | 2 |
Noncanonical E2 recruitment by the autophagy E1 revealed by Atg7-Atg3 and Atg7-Atg10 structures. Kaiser, S.E., Mao, K., Taherbhoy, A.M. et al. Nat Struct Mol Biol (2012) 19:1242-1249. DOI 10.1038/nsmb.2415 · 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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