4GSK: Atg7-Atg10 crosslinked complex

Crystal structure of an Atg7-Atg10 crosslinked complex. Determined by X-ray diffraction at 2.9 Å resolution. Released 14 Nov 2012.

Method
X-ray diffraction
Resolution
2.9 Å
Organism
Saccharomyces cerevisiae
Chains
4
Atoms
11,408
Mol. weight
179.68 kDa
Ligands
ZN
Released
14 Nov 2012

Explore 4GSK in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

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.

Chain A: 26 helices, 33 β-strands

ElementResiduesLengthSheet
β-strand5-621
β-strand1012
β-strand14-1743
α-helix19-2911
β-strand39-4684
β-strand5715
β-strand59-6243
α-helix64-663
β-strand78-87104
α-helix90-956
α-helix98-11518
α-helix117-1193
β-strand123-13084
β-strand135-146124
β-strand152-15761
α-helix159-1646
α-helix165-17410
β-strand180-18341
β-strand189-19021
α-helix194-2007
β-strand202-20651
β-strand20915
β-strand21612
α-helix219-22911
β-strand235-24171
β-strand248-25581
β-strand269-27354
α-helix2741
β-strand27516
β-strand28116
β-strand284-28744
α-helix294-30815
α-helix309-3135
α-helix320-3234
β-strand326-33057
α-helix334-34512
β-strand350-35567
β-strand35818
α-helix363-3653
α-helix372-3743
β-strand37818
α-helix379-39012
β-strand395-40067
α-helix404-4052
α-helix413-42816
β-strand432-43547
α-helix444-4529
β-strand456-46277
β-strand466-47167
α-helix486-4883
α-helix512-52918
α-helix532-5343
β-strand54019
β-strand54319
β-strand548-55257
β-strand557-56157
α-helix574-58310
α-helix585-5939
α-helix595-6028
Chain B: 26 helices, 33 β-strands
ElementResiduesLengthSheet
β-strand5-6210
β-strand10111
β-strand14-17412
α-helix19-2911
β-strand40-46713
β-strand57114
β-strand59-62412
α-helix64-674
β-strand78-871013
α-helix90-956
α-helix98-11518
α-helix117-1193
β-strand123-130813
β-strand135-1461213
β-strand151-157710
α-helix159-1646
α-helix165-17410
β-strand180-183410
β-strand189-191310
α-helix194-2007
β-strand202-206510
β-strand209114
β-strand216111
α-helix219-22911
β-strand235-241710
β-strand248-256910
β-strand269-273513
α-helix274-2752
β-strand284-287413
α-helix289-2924
α-helix294-30815
α-helix309-3135
α-helix320-3245
β-strand326-330515
α-helix334-34512
β-strand350-354515
β-strand358116
α-helix363-3664
α-helix372-3743
β-strand378116
α-helix379-39012
β-strand395-399515
α-helix404-4052
α-helix413-42917
β-strand432-435415
β-strand439117
α-helix440-45213
β-strand456-462715
β-strand466-472715
β-strand505117
α-helix512-52918
β-strand539-540218
β-strand543-544218
β-strand548-552515
β-strand557-561515
α-helix564-5663
α-helix574-58310
α-helix585-5939
α-helix595-6028
Chain Y: 4 helices, 6 β-strands
ElementResiduesLengthSheet
α-helix4-1613
β-strand26-31613
β-strand38-42513
α-helix43-453
α-helix46-549
β-strand59-701213
β-strand75-871313
β-strand92-97613
β-strand128-129213
α-helix149-1579
Chain Z: 6 helices, 6 β-strands
ElementResiduesLengthSheet
α-helix4-1613
β-strand26-3164
β-strand38-4254
α-helix43-453
α-helix46-5510
β-strand59-70124
β-strand75-87134
β-strand92-9764
β-strand128-12924
α-helix149-1546
α-helix155-1595
α-helix160-1623

Molecules and chains

MoleculeChainsTypeLengthOrganismUniProt
Ubiquitin-like modifier-activating enzyme ATG7A, Bprotein615Saccharomyces cerevisiaeP38862 (AlphaFold model)
Ubiquitin-like-conjugating enzyme ATG10Y, Zprotein173Saccharomyces cerevisiaeQ07879 (AlphaFold model)
Sequence of entity 1 (A, B), FASTA
>4GSK_1 Ubiquitin-like modifier-activating enzyme ATG7 (chains A, B)
GSMSSERVLSYAPAFKSFLDTSFFQELSRLKLDVLKLDSTSQPLTVNLDLHNIPKSADQV
PLFLTNRSFEKHNNKRTNEVPLQGSIFNFNVLDEFKNLDKQLFLHQRALECWEDGIKDIN
KCVSFVIISFADLKKYRFYYWLGVPCFQRPSSTVLHVRPEPSLKGLFSKCQKWFDVNYSK
WVCILDADDEIVNYDKSIIRKTKVLAIRDTSTMENVPSALTKNFLSVLQYDVPDLIDFKL
LIIRQNEGSFALNATFASIDPQSSSSNPDMKVSGWERNVQGKLAPRVVDLSSLLDPLKIA
DQSVDLNLKLMKWRILPDLNLDIIKNTKVLLLGAGTLGCYVSRALIAWGVRKITFVDNGT
VSYSNPVRQALYNFEDAGKPKAELAAASLKRIFPLMDATGVKLSIPMIGHKLVNEEAQHK
DFDRLRALIKEHDIIFLLVDSRESRWLPSLLSNIENKTVINAALGFDSYLVMRHGNRDEQ
SSKQLGCYFCHDVVAPTDSLTDRTLDQMCTVTRPGVAMMASSLAVELMTSLLQTKYSGSE
TTVLGDIPHQIRGFLHNFSILKLETPAYEHCPACSPKVIEAFTDLGWEFVKKALEHPLYL
EEISGLSVIKQEVER
Sequence of entity 2 (Y, Z), FASTA
>4GSK_2 Ubiquitin-like-conjugating enzyme ATG10 (chains Y, Z)
GSGGSGMIPYQEWHSQLQSLYDSQIFHNWALSQDVHLNDEKDGLLLRLIPTRQLQKNTER
IENKLLNHIELYLTYSKVYNEPLLLLRIWEEKSIDGIPMTKLMLPTDIESLLDVQGKFQL
GLDTIINLEGSVWYSFHPCDTSSIVGDQAEFMSTYLRRWVSIFIFSWLGYEDS

Ligands and cofactors

IDNameFormulaCopies
ZNZinc ionZn2

Primary citation

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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