Crystal structure of the human KLHL11-Cul3 complex at 3.1A resolution. Determined by X-ray diffraction at 3.1 Å resolution. Released 9 May 2012.
Explore 4APF in 3D Show helices and sheets RCSB PDB PDBe
4APF contains 48 α-helices and 3 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 |
|---|---|---|---|
| α-helix | 75-90 | 16 | |
| β-strand | 96-99 | 4 | 1 |
| β-strand | 107-110 | 4 | 1 |
| α-helix | 112-118 | 7 | |
| α-helix | 122-127 | 6 | |
| α-helix | 132-135 | 4 | |
| β-strand | 138-139 | 2 | 1 |
| α-helix | 151-163 | 13 | |
| α-helix | 172-182 | 11 | |
| α-helix | 186-198 | 13 | |
| α-helix | 204-214 | 11 | |
| α-helix | 218-230 | 13 | |
| α-helix | 232-235 | 4 | |
| α-helix | 239-243 | 5 | |
| α-helix | 246-253 | 8 | |
| α-helix | 264-276 | 13 | |
| α-helix | 278-281 | 4 | |
| α-helix | 285-291 | 7 | |
| α-helix | 294-296 | 3 | |
| α-helix | 299-301 | 3 | |
| α-helix | 302-306 | 5 | |
| α-helix | 310-314 | 5 | |
| α-helix | 316-331 | 16 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| α-helix | 27-45 | 19 | |
| α-helix | 49-51 | 3 | |
| α-helix | 54-66 | 13 | |
| α-helix | 70-84 | 15 | |
| α-helix | 85-90 | 6 | |
| α-helix | 91-95 | 5 | |
| α-helix | 101-122 | 22 | |
| α-helix | 124-126 | 3 | |
| α-helix | 127-131 | 5 | |
| α-helix | 132-133 | 2 | |
| α-helix | 139-147 | 9 | |
| α-helix | 148-152 | 5 | |
| α-helix | 156-173 | 18 | |
| α-helix | 180-192 | 13 | |
| α-helix | 199-201 | 3 | |
| α-helix | 202-206 | 5 | |
| α-helix | 207-227 | 21 | |
| α-helix | 230-251 | 22 | |
| α-helix | 254-256 | 3 | |
| α-helix | 257-264 | 8 | |
| α-helix | 265-269 | 5 | |
| α-helix | 270-272 | 3 | |
| α-helix | 273-277 | 5 | |
| α-helix | 283-289 | 7 | |
| α-helix | 293-303 | 11 | |
| α-helix | 309-325 | 17 | |
| α-helix | 345-358 | 14 | |
| α-helix | 364-378 | 15 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| Kelch-like protein 11 | A | protein | 297 | HOMO SAPIENS | Q9NVR0 (AlphaFold model) |
| Cullin 3 | B | protein | 388 | HOMO SAPIENS | Q13618 (AlphaFold model) |
>4APF_1 KELCH-LIKE PROTEIN 11 (chains A) MHHHHHHSSGVDLGTENLYFQSMEAEDFECSSHCSELSWRQNEQRRQGLFCDITLCFGGA GGREFRAHRSVLAAATEYFTPLLSGQFSESRSGRVEMRKWSSEPGPEPDTVEAVIEYMYT GRIRVSTGSVHEVLELADRFLLIRLKEFCGEFLKKKLHLSNCVAIHSLAHMYTLSQLALK AADMIRRNFHKVIQDEEFYTLPFHLIRDWLSDLEITVDSEEVLFETVLKWVQRNAEERER YFEELFKLLRLSQMKPTYLTRHVKPERLVANNEVCVKLVADAVERHALRAENIQSGT
>4APF_2 CULLIN 3 (chains B) MTMDEKYVNSIWDLLKNAIQEIQRKNNSGLSFEELYRNAYTMVLHKHGEKLYTGLREVVT EHLINKVREDVLNSLNNNFLQTLNQAWNDHQTAMVMIRDILMYMDRVYVQQNNVENVYNL GLIIFRDQVVRYGCIRDHLRQTLLDMIARERKGEVVDRGAIRNACQMLMILGLEGRSVYE EDFEAPFLEMSAEFFQMESQKFLAENSASVYIKKVEARINEEIERVMHCLDKSTEEPIVK VVERELISKHMKTIVEMENSGLVHMLKNGKTEDLGCMYKLFSRVPNGLKTMCECMSSYLR EQGKALVSEEGEGKNPVDYRQGLDDLKSRFDRFLLESFNNDRLFKQTIAGDFEYFLNLNS RSPEYLAENLYFQSHHHHHHDYKDDDDK
Structural Basis for Cul3 Assembly with the Btb-Kelch Family of E3 Ubiquitin Ligases. Canning, P., Cooper, C.D.O., Krojer, T. et al. J Biol Chem (2013) 288:7803. DOI 10.1074/JBC.M112.437996 · PubMed
Other PDB entries of the same protein (UniProt Q9NVR0 (AlphaFold model), which also has an AlphaFold model), best resolution first:
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