Crystal structure of F-box protein in the ternary complex with adaptor protein Skp1(DL) and its substrate. Determined by X-ray diffraction at 2.53 Å resolution. Released 26 Apr 2023.
Explore 8GRF in 3D Show helices and sheets RCSB PDB PDBe
8GRF contains 83 α-helices and 35 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 | 26-48 | 23 | |
| β-strand | 52-57 | 6 | 1 |
| α-helix | 58-61 | 4 | |
| β-strand | 69-72 | 4 | 2 |
| β-strand | 76-79 | 4 | 3 |
| β-strand | 83-86 | 4 | 3 |
| β-strand | 89 | 1 | 3 |
| α-helix | 91-97 | 7 | |
| β-strand | 100 | 1 | 4 |
| β-strand | 107 | 1 | 4 |
| α-helix | 109-118 | 10 | |
| α-helix | 124-136 | 13 | |
| α-helix | 139-141 | 3 | |
| α-helix | 142-148 | 7 | |
| α-helix | 157-167 | 11 | |
| α-helix | 168-171 | 4 | |
| α-helix | 173-180 | 8 | |
| α-helix | 184-186 | 3 | |
| α-helix | 187-214 | 28 | |
| α-helix | 218-221 | 4 | |
| α-helix | 228-236 | 9 | |
| α-helix | 241-253 | 13 | |
| α-helix | 262-272 | 11 | |
| α-helix | 277-288 | 12 | |
| α-helix | 296-311 | 16 | |
| α-helix | 317-329 | 13 | |
| β-strand | 337 | 1 | 5 |
| α-helix | 347-359 | 13 | |
| α-helix | 364-383 | 20 | |
| β-strand | 391 | 1 | 5 |
| α-helix | 393-395 | 3 | |
| α-helix | 397-403 | 7 | |
| α-helix | 409-411 | 3 | |
| α-helix | 412-434 | 23 | |
| α-helix | 436-438 | 3 | |
| β-strand | 442-444 | 3 | 6 |
| α-helix | 446-459 | 14 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| α-helix | 23-25 | 3 | |
| α-helix | 26-48 | 23 | |
| β-strand | 52-57 | 6 | 1 |
| α-helix | 58-61 | 4 | |
| β-strand | 69-72 | 4 | 6 |
| β-strand | 76-79 | 4 | 7 |
| β-strand | 83-86 | 4 | 7 |
| β-strand | 89 | 1 | 7 |
| α-helix | 91-97 | 7 | |
| β-strand | 100 | 1 | 8 |
| β-strand | 107 | 1 | 8 |
| α-helix | 108 | 1 | |
| α-helix | 109-118 | 10 | |
| α-helix | 121-123 | 3 | |
| α-helix | 124-136 | 13 | |
| α-helix | 139-141 | 3 | |
| α-helix | 142-150 | 9 | |
| α-helix | 157-167 | 11 | |
| α-helix | 168-171 | 4 | |
| α-helix | 173-179 | 7 | |
| α-helix | 184-186 | 3 | |
| α-helix | 187-214 | 28 | |
| α-helix | 228-236 | 9 | |
| α-helix | 241-253 | 13 | |
| α-helix | 262-272 | 11 | |
| α-helix | 277-288 | 12 | |
| α-helix | 296-310 | 15 | |
| α-helix | 317-330 | 14 | |
| β-strand | 337 | 1 | 9 |
| α-helix | 347-359 | 13 | |
| α-helix | 364-383 | 20 | |
| β-strand | 391 | 1 | 9 |
| α-helix | 394-403 | 10 | |
| α-helix | 409-411 | 3 | |
| α-helix | 412-433 | 22 | |
| α-helix | 436-438 | 3 | |
| β-strand | 442-444 | 3 | 2 |
| α-helix | 446-458 | 13 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| α-helix | 8-10 | 3 | |
| α-helix | 13-22 | 10 | |
| α-helix | 24-27 | 4 | |
| α-helix | 32-49 | 18 | |
| α-helix | 55-70 | 16 | |
| α-helix | 72-79 | 8 | |
| β-strand | 86 | 1 | 10 |
| α-helix | 94-96 | 3 | |
| β-strand | 97 | 1 | 10 |
| α-helix | 104-112 | 9 | |
| α-helix | 114-116 | 3 | |
| β-strand | 117-118 | 2 | 11 |
| β-strand | 147-157 | 11 | 12 |
| β-strand | 170-177 | 8 | 11 |
| α-helix | 182-188 | 7 | |
| β-strand | 189-195 | 7 | 12 |
| β-strand | 202-204 | 3 | 12 |
| α-helix | 210-213 | 4 | |
| β-strand | 218-226 | 9 | 11 |
| α-helix | 233-236 | 4 | |
| β-strand | 243-252 | 10 | 12 |
| β-strand | 264-270 | 7 | 11 |
| β-strand | 280-285 | 6 | 11 |
| α-helix | 291-293 | 3 | |
| α-helix | 297-314 | 18 | |
| α-helix | 318-319 | 2 | |
| β-strand | 341-344 | 4 | 11 |
| α-helix | 349-351 | 3 | |
| α-helix | 353-358 | 6 | |
| α-helix | 360-361 | 2 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| β-strand | 5-10 | 6 | 13 |
| β-strand | 15-19 | 5 | 13 |
| α-helix | 20-23 | 4 | |
| α-helix | 27-30 | 4 | |
| β-strand | 77-79 | 3 | 13 |
| α-helix | 84-96 | 13 | |
| α-helix | 108-113 | 6 | |
| α-helix | 114-117 | 4 | |
| α-helix | 118-123 | 6 | |
| α-helix | 128-140 | 13 | |
| α-helix | 144-158 | 15 | |
| α-helix | 163-170 | 8 | |
| α-helix | 178-190 | 13 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| Citrate synthase | A, B | protein | 460 | Saccharomyces cerevisiae | P08679 (AlphaFold model) |
| F-box protein UCC1 | C | protein | 369 | Saccharomyces cerevisiae | Q05947 (AlphaFold model) |
| E3 ubiquitin ligase complex SCF subunit | D | protein | 194 | Saccharomyces cerevisiae | P52286 (AlphaFold model) |
>8GRF_1 Citrate synthase (chains A, B) MTVPYLNSNRNVASYLQSNSSQEKTLKERFSEIYPIHAQDVRQFVKEHGKTKISDVLLEQ VYGGMRGIPGSVWEGSVLDPEDGIRFRGRTIADIQKDLPKAKGSSQPLPEALFWLLLTGE VPTQAQVENLSADLMSRSELPSHVVQLLDNLPKDLHPMAQFSIAVTALESESKFAKAYAQ GISKQDYWSYTFEDSLDLLGKLPVIAAKIYRNVFKDGKMGEVDPNADYAKNLVNLIGSKD EDFVDLMRLYLTIHSDHEGGNVSAHTSHLVGSALSSPYLSLASGLNGLAGPLHGRANQEV LEWLFALKEEVNDDYSKDTIEKYLWDTLNSGRVIPGYGHAVLRKTDPRYMAQRKFAMDHF PDYELFKLVSSIYEVAPGVLTEHGKTKNPWPNVDAHSGVLLQYYGLKESSFYTVLFGVSR AFGILAQLITDRAIGASIERPKSYSTEKYKELVKNIESKL
>8GRF_2 F-box protein UCC1 (chains C) MNQSDSSLMDLPLEIHLSLLEYVPNELRAVNKYFYVLHNHSYKEKSLAWIAEDNYIWAVV KHSLCLYVKSLDPLRQHAREIIQETKEPGFNVPLCMTKYIADSWYIVYNALQYPGKIINM GWDKYTKSQDLNGSDSTSNFNSRPKERTLMQSLTALPVNFWSRKKDEPTPVNVWFYVKNA HVARYIPKIITEIGICNYGPKQIVASAGYINELITSEGIYCVNLGHLPRLYDEQIFEGTG TTHLPLELKAIDRTDSDVCINSDLVLLGYDFIPYQISKPWLLFRIEPVNSIEAIFNYSEC SFSYQFAWSLACLQSEEKISFPRDTIIGHGLPYKPSKLIRIFVYKHPEQKQDLGQEIALP NWNTPYLRR
>8GRF_3 E3 ubiquitin ligase complex SCF subunit (chains D) MVTSNVVLVSGEGERFTVDKKIAERSLLLKNYLNDMHDSNLQNNSDSESDSDSETNHKSK DNNNGDDDDEDDDEIVMPVPNVRSSVLQKVIEWAEHHRDSNFPDEDDDDSRKSAPVDSWD REFLKVDQEMLYEIILAANYLNIKPLLDAGCKVVAEMIRGRSPEEIRRTFNIVNDFTPEE EAAIRRENEWAEDR
Defective import of mitochondrial metabolic enzyme elicits ectopic metabolic stress. Nishio, K., Kawarasaki, T., Sugiura, Y. et al. Sci Adv (2023) 9:eadf1956-eadf1956. DOI 10.1126/sciadv.adf1956 · PubMed
Other PDB entries of the same protein (UniProt P08679 (AlphaFold model), which also has an AlphaFold model), best resolution first:
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