9FSK: HECT domain of Smurf1

Crystal structure of the HECT domain of Smurf1. Determined by X-ray diffraction at 2.75 Å resolution. Released 16 Apr 2025.

Method
X-ray diffraction
Resolution
2.75 Å
Organism
Homo sapiens
Chains
4
Atoms
12,302
Mol. weight
175.9 kDa
Released
16 Apr 2025

Explore 9FSK in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

9FSK contains 96 α-helices and 62 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: 24 helices, 15 β-strands

ElementResiduesLengthSheet
α-helix378-39114
β-strand398-40361
α-helix408-41811
α-helix421-4244
β-strand427-43261
α-helix444-45512
α-helix458-4603
β-strand463-46532
β-strand473-47532
α-helix479-4813
α-helix485-50117
β-strand51012
α-helix512-5187
α-helix521-5244
α-helix525-5273
α-helix528-5314
α-helix533-54412
β-strand55413
β-strand556-56164
β-strand564-56964
α-helix574-5763
β-strand57813
α-helix584-59613
α-helix601-61212
α-helix617-6204
α-helix625-6339
β-strand63515
α-helix640-6456
β-strand647-65046
α-helix657-66812
α-helix671-68212
β-strand68715
α-helix692-6943
β-strand707-71156
α-helix719-7202
β-strand721-72336
α-helix724-7263
β-strand728-73146
α-helix737-74913
Chain B: 24 helices, 17 β-strands
ElementResiduesLengthSheet
α-helix379-39214
β-strand398-40367
α-helix408-41811
α-helix421-4244
β-strand427-43267
α-helix444-45512
α-helix458-4603
β-strand463-46538
β-strand473-47538
α-helix477-4815
α-helix485-50117
β-strand51018
α-helix512-5187
α-helix521-5244
α-helix525-5273
α-helix528-5314
α-helix533-54412
β-strand55419
β-strand556-557210
β-strand560-561211
β-strand564-565211
β-strand568-569210
α-helix574-5763
β-strand57819
α-helix584-59613
α-helix601-61212
α-helix617-6204
α-helix625-6339
β-strand635112
α-helix640-6456
β-strand647-650413
α-helix657-66812
α-helix671-68212
β-strand687112
α-helix691-6944
β-strand707-711513
α-helix719-7202
β-strand721-723313
α-helix724-7263
β-strand728-731413
α-helix737-74812
Chain C: 23 helices, 15 β-strands
ElementResiduesLengthSheet
α-helix378-39114
β-strand398-403614
α-helix408-41811
α-helix421-4244
β-strand427-432614
α-helix444-45512
α-helix458-4603
β-strand463-465315
β-strand473-475315
α-helix479-4813
α-helix485-50117
β-strand510115
α-helix512-5198
α-helix521-5244
α-helix528-5314
α-helix533-54412
β-strand554116
β-strand556-558317
β-strand567-569317
β-strand578116
α-helix584-59714
α-helix601-61212
α-helix617-6204
α-helix625-6339
β-strand635118
α-helix638-6392
α-helix640-6456
β-strand647-650419
α-helix657-66711
α-helix671-68212
β-strand687118
α-helix692-6943
β-strand707-711519
α-helix719-7202
β-strand721-723319
α-helix724-7263
β-strand728-731419
α-helix737-74913
Chain D: 25 helices, 15 β-strands
ElementResiduesLengthSheet
α-helix378-39215
β-strand398-403620
α-helix408-41811
α-helix421-4244
β-strand427-432620
α-helix444-45512
α-helix458-4603
β-strand463-465321
β-strand473-475321
α-helix479-4813
α-helix485-50117
β-strand510121
α-helix512-5187
α-helix521-5244
α-helix525-5273
α-helix528-5314
α-helix533-54412
β-strand554122
β-strand556-557223
β-strand568-569223
α-helix574-5763
β-strand578122
α-helix584-59714
α-helix601-61212
α-helix617-6204
α-helix625-6339
β-strand635124
α-helix638-6392
α-helix640-6456
β-strand647-650425
α-helix658-66811
α-helix671-68212
β-strand687124
α-helix704-7063
β-strand707-711525
α-helix719-7202
β-strand721-723325
α-helix724-7263
β-strand728-731425
α-helix737-74812

Molecules and chains

MoleculeChainsTypeLengthOrganismUniProt
E3 ubiquitin-protein ligase SMURF1A, B, C, Dprotein377Homo sapiensQ9HCE7 (AlphaFold model)
Sequence of entity 1 (A, B, C, D), FASTA
>9FSK_1 E3 ubiquitin-protein ligase SMURF1 (chains A, B, C, D)
GPDLVQKLKVLRHELSLQQPQAGHCRIEVSREEIFEESYRQIMKMRPKDLKKRLMVKFRG
EEGLDYGGVAREWLYLLCHEMLNPYYGLFQYSTDNIYMLQINPDSSINPDHLSYFHFVGR
IMGLAVFHGHYINGGFTVPFYKQLLGKPIQLSDLESVDPELHKSLVWILENDITPVLDHT
FCVEHNAFGRILQHELKPNGRNVPVTEENKKEYVRLYVNWRFMRGIEAQFLALQKGFNEL
IPQHLLKPFDQKELELIIGGLDKIDLNDWKSNTRLKHCVADSNIVRWFWQAVETFDEERR
ARLLQFVTGSTRVPLQGFKALQGSTGAAGPRLFTIHLIDANTDNLPKAHTCFNRIDIPPY
ESYEKLYEKLLTAVEET

Primary citation

Therapeutic potential of allosteric HECT E3 ligase inhibition. Rothman, A.M.K., Florentin, A., Zink, F. et al. Cell (2025) 188:2603. DOI 10.1016/j.cell.2025.03.001 · PubMed

Other PDB entries of the same protein (UniProt Q9HCE7 (AlphaFold model), which also has an AlphaFold model), best resolution first:

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