Crystal structure of the SPOP BTB domain complexed with the Cul3 N-terminal domain. Determined by X-ray diffraction at 2.4 Å resolution. Released 30 May 2012.
Explore 4EOZ in 3D Show helices and sheets RCSB PDB PDBe
4EOZ contains 65 α-helices and 6 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 |
|---|---|---|---|
| α-helix | 180-184 | 5 | |
| α-helix | 186-196 | 11 | |
| β-strand | 202-206 | 5 | 1 |
| β-strand | 209-213 | 5 | 1 |
| α-helix | 215-221 | 7 | |
| α-helix | 223-230 | 8 | |
| α-helix | 234-238 | 5 | |
| β-strand | 240-243 | 4 | 1 |
| α-helix | 248-260 | 13 | |
| α-helix | 266-268 | 3 | |
| α-helix | 270-279 | 10 | |
| α-helix | 283-290 | 8 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| α-helix | 26-45 | 20 | |
| α-helix | 49-51 | 3 | |
| α-helix | 54-66 | 13 | |
| α-helix | 70-84 | 15 | |
| α-helix | 85-89 | 5 | |
| α-helix | 90-94 | 5 | |
| α-helix | 101-122 | 22 | |
| α-helix | 124-129 | 6 | |
| α-helix | 132-134 | 3 | |
| α-helix | 139-147 | 9 | |
| α-helix | 148-152 | 5 | |
| α-helix | 155-173 | 19 | |
| 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 | 257-265 | 9 | |
| α-helix | 266-270 | 5 | |
| α-helix | 273-277 | 5 | |
| α-helix | 284-287 | 4 | |
| α-helix | 293-303 | 11 | |
| α-helix | 309-323 | 15 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| α-helix | 181-184 | 4 | |
| α-helix | 186-196 | 11 | |
| β-strand | 202-206 | 5 | 2 |
| β-strand | 209-213 | 5 | 2 |
| α-helix | 215-221 | 7 | |
| α-helix | 223-230 | 8 | |
| α-helix | 234-238 | 5 | |
| β-strand | 240-243 | 4 | 2 |
| α-helix | 248-260 | 13 | |
| α-helix | 266-279 | 14 | |
| α-helix | 283-293 | 11 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| α-helix | 25-45 | 21 | |
| α-helix | 54-66 | 13 | |
| α-helix | 70-83 | 14 | |
| α-helix | 84-89 | 6 | |
| α-helix | 90-94 | 5 | |
| α-helix | 101-122 | 22 | |
| α-helix | 124-125 | 2 | |
| α-helix | 126-130 | 5 | |
| α-helix | 136-138 | 3 | |
| α-helix | 139-147 | 9 | |
| α-helix | 148-152 | 5 | |
| α-helix | 155-173 | 19 | |
| α-helix | 180-192 | 13 | |
| α-helix | 199-201 | 3 | |
| α-helix | 202-206 | 5 | |
| α-helix | 207-225 | 19 | |
| α-helix | 230-250 | 21 | |
| α-helix | 254-256 | 3 | |
| α-helix | 257-268 | 12 | |
| α-helix | 270-272 | 3 | |
| α-helix | 273-278 | 6 | |
| α-helix | 284-290 | 7 | |
| α-helix | 294-303 | 10 | |
| α-helix | 309-323 | 15 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| Speckle-type POZ protein | A, C | protein | 145 | Homo sapiens | O43791 (AlphaFold model) |
| Cullin-3 | B, D | protein | 364 | Homo sapiens | Q13618 (AlphaFold model) |
>4EOZ_1 Speckle-type POZ protein (chains A, C) GSNMVKVPECRLADELGGLWENSRFTDCCLCVAGQEFQAHKAILAARSPVFSAMFEHEME ESKKNRVEINDVEPEVFKEMMCFIYTGKAPNLDKMADDLLAAADKYALERLKVMCEDALC SNLSVENAAEILILADLHSADQLKT
>4EOZ_2 Cullin-3 (chains B, D) GSAFPMTMDEKYVNSIWDLLKNAIQEIQRKNNSGLSFEELYRNAYTMVLHKHGEKLYTGL REVVTEHLINKVREDVLNSLNNNFLQTLNQAWNDHQTAMVMIRDILMYMDRVYVQQNNVE NVYNLGLIIFRDQVVRYGCIRDHLRQTLLDMIARERKGEVVDRGAIRNACQMLMILGLEG RSVYEEDFEAPFLEMSAEFFQMESQKFLAENSASVYIKKVEARINEEIERVMHCLDKSTE EPIVKVVERELISKHMKTIVEMENSGLVHMLKNGKTEDLGCMYKLFSRVPNGLKTMCECM SSYLREQGKALVSEEGEGKNPVDYRQGLDDLKSRFDRFLLESFNNDRLFKQTIAGDFEYF LNLN
Adaptor protein self-assembly drives the control of a cullin-RING ubiquitin ligase. Errington, W.J., Khan, M.Q., Bueler, S.A. et al. Structure (2012) 20:1141-1153. DOI 10.1016/j.str.2012.04.009 · PubMed
Other PDB entries of the same protein (UniProt O43791 (AlphaFold model), which also has an AlphaFold model), best resolution first:
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