4GSL: Atg7-Atg3 crosslinked complex

Crystal structure of an Atg7-Atg3 crosslinked complex. Determined by X-ray diffraction at 2.7 Å resolution. Released 14 Nov 2012.

Method
X-ray diffraction
Resolution
2.7 Å
Organism
Saccharomyces cerevisiae
Chains
4
Atoms
12,543
Mol. weight
211.47 kDa
Ligands
ZN
Released
14 Nov 2012

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

Secondary structure: helices and β-sheets

4GSL contains 75 α-helices and 86 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, 31 β-strands

ElementResiduesLengthSheet
β-strand5-621
β-strand1012
β-strand14-1743
α-helix19-279
β-strand37-46104
β-strand5715
β-strand59-6243
α-helix64-674
α-helix771
β-strand78-87104
α-helix90-945
α-helix98-11316
α-helix117-1193
β-strand123-13084
β-strand135-146124
β-strand151-15771
α-helix164-17411
β-strand180-18341
β-strand189-19131
α-helix194-2007
β-strand202-20651
β-strand20915
β-strand21612
α-helix218-22912
β-strand235-24171
β-strand248-25691
α-helix259-2613
β-strand269-27354
α-helix274-2752
β-strand284-28744
α-helix289-2924
α-helix294-31219
α-helix319-3235
β-strand326-33056
α-helix334-34512
β-strand350-35456
β-strand35817
α-helix363-3653
α-helix372-3743
β-strand37817
α-helix379-39012
β-strand395-39956
α-helix413-42917
β-strand432-43546
α-helix440-4423
α-helix444-4529
β-strand456-46276
β-strand466-47166
α-helix512-53019
α-helix532-5343
β-strand539-54028
β-strand543-54428
β-strand548-55256
β-strand557-56156
α-helix574-59320
α-helix595-6028
α-helix604-6063
Chain B: 24 helices, 34 β-strands
ElementResiduesLengthSheet
β-strand5-629
β-strand10110
β-strand13-17511
α-helix19-3012
β-strand38-46912
β-strand57113
β-strand58-62511
α-helix64-674
β-strand78-871012
α-helix90-956
α-helix98-11518
α-helix117-1193
β-strand123-130812
β-strand135-1461212
β-strand151-15779
α-helix164-17411
β-strand180-18349
β-strand189-19029
α-helix194-2007
β-strand202-20659
β-strand209113
β-strand216110
α-helix218-22912
β-strand235-24179
β-strand248-25699
β-strand269-273512
α-helix274-2752
β-strand281114
β-strand284-287412
α-helix289-2924
α-helix294-31219
α-helix319-3235
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-helix413-42917
β-strand432-435415
α-helix444-45310
β-strand456-462715
β-strand466-471615
β-strand483117
α-helix484-4852
α-helix513-53018
α-helix532-5343
β-strand539-540218
β-strand543-544218
β-strand548-552515
β-strand557-561515
β-strand564117
α-helix565-5662
α-helix574-59320
α-helix595-6028
Chain C: 12 helices, 11 β-strands
ElementResiduesLengthSheet
α-helix22-254
α-helix30-4314
β-strand48-49219
β-strand56120
α-helix64-663
β-strand69-76819
α-helix80-823
α-helix133-1397
β-strand141114
β-strand167-175919
β-strand182-189819
α-helix1941
β-strand195119
α-helix196-1972
α-helix198-2025
α-helix207-2137
β-strand215-218419
β-strand222120
β-strand227-231519
α-helix239-2435
α-helix283-2853
α-helix286-29712
β-strand301119
Chain D: 13 helices, 10 β-strands
ElementResiduesLengthSheet
α-helix22-254
α-helix30-4314
β-strand48-49221
α-helix50-512
β-strand56122
β-strand68-76921
α-helix80-823
α-helix133-1386
β-strand167-1761021
β-strand181-189921
α-helix1941
β-strand195121
α-helix196-1972
α-helix198-2014
α-helix202-2043
α-helix207-2104
β-strand215-218421
β-strand222122
β-strand227-231521
α-helix239-2446
α-helix283-2853
α-helix286-29712
β-strand301121

Molecules and chains

MoleculeChainsTypeLengthOrganismUniProt
Ubiquitin-like modifier-activating enzyme ATG7A, Bprotein615Saccharomyces cerevisiaeP38862 (AlphaFold model)
Autophagy-related protein 3C, Dprotein312Saccharomyces cerevisiaeP40344 (AlphaFold model)
Sequence of entity 1 (A, B), FASTA
>4GSL_1 Ubiquitin-like modifier-activating enzyme ATG7 (chains A, B)
GSMSSERVLSYAPAFKSFLDTSFFQELSRLKLDVLKLDSTCQPLTVNLDLHNIPKSADQV
PLFLTNRSFEKHNNKRTNEVPLQGSIFNFNVLDEFKNLDKQLFLHQRALECWEDGIKDIN
KCVSFVIISFADLKKYRFYYWLGVPCFQRPSSTVLHVRPEPSLKGLFSKCQKWFDVNYSK
WVCILDADDEIVNYDKCIIRKTKVLAIRDTSTMENVPSALTKNFLSVLQYDVPDLIDFKL
LIIRQNEGSFALNATFASIDPQSSSSNPDMKVSGWERNVQGKLAPRVVDLSSLLDPLKIA
DQSVDLNLKLMKWRILPDLNLDIIKNTKVLLLGAGTLGCYVSRALIAWGVRKITFVDNGT
VSYSNPVRQALYNFEDCGKPKAELAAASLKRIFPLMDATGVKLSIPMIGHKLVNEEAQHK
DFDRLRALIKEHDIIFLLVDSRESRWLPSLLSNIENKTVINAALGFDSYLVMRHGNRDEQ
SSKQLGCYFCHDVVAPTDSLTDRTLDQMCTVTRPGVAMMASSLAVELMTSLLQTKYSGSE
TTVLGDIPHQIRGFLHNFSILKLETPAYEHCPACSPKVIEAFTDLGWEFVKKALEHPLYL
EEISGLSVIKQEVER
Sequence of entity 2 (C, D), FASTA
>4GSL_2 Autophagy-related protein 3 (chains C, D)
GSMIRSTLSSWREYLTPITHKSTFLTTGQITPEEFVQAGDYLAHMFPTWKWNEESSDISY
RDFLPKNKQFLIIRKVPADKRAEQAVEVEGPDVIMKGFAEDGDEDDVLEYIGSETEHVQS
TPAGGTKDSSIDDIDELIQDMEIKEEDENDDTEEFNAKGGLAKDMAQERYYDLYIAYSTS
YRVPKMYIVGFNSNGSPLSPEQMFEDISADYRTKTATIEKLPFYKNSVLSVSIHPCKHAN
VMKILLDKVRVVRQRRRKELQEEQELDGVGDWEDLQDDIDDSLRVDQYLIVFLKFITSVT
PSIQHDYTMEGW

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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