CAND1-CUL1-RBX1-DCNL1. Determined by electron microscopy at 3.2 Å resolution. Released 28 Jun 2023.
Explore 8OR2 in 3D Show helices and sheets RCSB PDB PDBe
8OR2 contains 114 α-helices and 20 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 | 25-32 | 8 | |
| α-helix | 39-53 | 15 | |
| α-helix | 87-106 | 20 | |
| α-helix | 116-136 | 21 | |
| α-helix | 138-141 | 4 | |
| α-helix | 159-172 | 14 | |
| α-helix | 175-190 | 16 | |
| α-helix | 198-210 | 13 | |
| α-helix | 226-228 | 3 | |
| α-helix | 229-233 | 5 | |
| α-helix | 234-254 | 21 | |
| α-helix | 257-278 | 22 | |
| α-helix | 283-295 | 13 | |
| α-helix | 297-299 | 3 | |
| α-helix | 300-312 | 13 | |
| α-helix | 316-327 | 12 | |
| α-helix | 334-354 | 21 | |
| α-helix | 365-384 | 20 | |
| α-helix | 389-404 | 16 | |
| α-helix | 407-412 | 6 | |
| α-helix | 417-430 | 14 | |
| β-strand | 431 | 1 | 1 |
| α-helix | 443-453 | 11 | |
| α-helix | 460-475 | 16 | |
| β-strand | 479 | 1 | 1 |
| α-helix | 482-495 | 14 | |
| α-helix | 499-524 | 26 | |
| β-strand | 536-541 | 6 | 2 |
| α-helix | 548-552 | 5 | |
| α-helix | 560-571 | 12 | |
| β-strand | 577-592 | 16 | 2 |
| β-strand | 599-604 | 6 | 2 |
| α-helix | 605-611 | 7 | |
| α-helix | 622-629 | 8 | |
| α-helix | 633-645 | 13 | |
| β-strand | 681-683 | 3 | 2 |
| α-helix | 691-721 | 31 | |
| β-strand | 724-726 | 3 | 3 |
| α-helix | 727-737 | 11 | |
| α-helix | 746-758 | 13 | |
| β-strand | 762-764 | 3 | 3 |
| β-strand | 771-774 | 4 | 3 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| β-strand | 23-35 | 13 | 2 |
| α-helix | 36-40 | 5 | |
| α-helix | 52-53 | 2 | |
| α-helix | 54-58 | 5 | |
| β-strand | 70-71 | 2 | 4 |
| β-strand | 79-80 | 2 | 4 |
| α-helix | 81-90 | 10 | |
| β-strand | 93-94 | 2 | 5 |
| β-strand | 99-100 | 2 | 5 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| α-helix | 5-14 | 10 | |
| α-helix | 20-22 | 3 | |
| α-helix | 25-35 | 11 | |
| α-helix | 43-56 | 14 | |
| α-helix | 62-77 | 16 | |
| α-helix | 81-95 | 15 | |
| α-helix | 100-116 | 17 | |
| α-helix | 128-141 | 14 | |
| α-helix | 149-164 | 16 | |
| α-helix | 170-172 | 3 | |
| α-helix | 173-180 | 8 | |
| α-helix | 181-185 | 5 | |
| α-helix | 189-205 | 17 | |
| α-helix | 212-225 | 14 | |
| α-helix | 233-244 | 12 | |
| α-helix | 250-252 | 3 | |
| α-helix | 257-263 | 7 | |
| α-helix | 271-284 | 14 | |
| α-helix | 291-303 | 13 | |
| α-helix | 347-362 | 16 | |
| α-helix | 368-373 | 6 | |
| α-helix | 376-382 | 7 | |
| α-helix | 388-405 | 18 | |
| α-helix | 424-442 | 19 | |
| α-helix | 448-464 | 17 | |
| α-helix | 473-485 | 13 | |
| α-helix | 491-506 | 16 | |
| α-helix | 510-512 | 3 | |
| α-helix | 514-516 | 3 | |
| α-helix | 517-528 | 12 | |
| α-helix | 533-550 | 18 | |
| α-helix | 562-564 | 3 | |
| α-helix | 565-576 | 12 | |
| α-helix | 583-599 | 17 | |
| α-helix | 607-620 | 14 | |
| α-helix | 625-636 | 12 | |
| α-helix | 645-647 | 3 | |
| α-helix | 652-656 | 5 | |
| α-helix | 657-659 | 3 | |
| α-helix | 664-680 | 17 | |
| α-helix | 687-694 | 8 | |
| β-strand | 702 | 1 | 6 |
| β-strand | 705 | 1 | 6 |
| α-helix | 707-722 | 16 | |
| α-helix | 734-742 | 9 | |
| α-helix | 750-765 | 16 | |
| α-helix | 772-779 | 8 | |
| α-helix | 793-809 | 17 | |
| α-helix | 814-825 | 12 | |
| α-helix | 832-845 | 14 | |
| α-helix | 857-865 | 9 | |
| α-helix | 871-886 | 16 | |
| α-helix | 888-901 | 14 | |
| α-helix | 906-919 | 14 | |
| α-helix | 922-925 | 4 | |
| α-helix | 930-940 | 11 | |
| α-helix | 945-958 | 14 | |
| α-helix | 963-976 | 14 | |
| α-helix | 979-990 | 12 | |
| α-helix | 1001-1013 | 13 | |
| α-helix | 1020-1036 | 17 | |
| α-helix | 1045-1056 | 12 | |
| β-strand | 1063-1066 | 4 | 7 |
| β-strand | 1073-1076 | 4 | 7 |
| α-helix | 1079-1091 | 13 | |
| α-helix | 1103-1112 | 10 | |
| α-helix | 1117-1130 | 14 | |
| α-helix | 1135-1139 | 5 | |
| α-helix | 1142-1153 | 12 | |
| α-helix | 1157-1158 | 2 | |
| α-helix | 1163-1184 | 22 | |
| α-helix | 1202-1204 | 3 | |
| α-helix | 1206-1209 | 4 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| α-helix | 66-72 | 7 | |
| α-helix | 100-108 | 9 | |
| α-helix | 134-149 | 16 | |
| α-helix | 153-165 | 13 | |
| β-strand | 173 | 1 | 8 |
| α-helix | 175-185 | 11 | |
| α-helix | 193-198 | 6 | |
| β-strand | 208 | 1 | 8 |
| α-helix | 210-222 | 13 | |
| α-helix | 240-250 | 11 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| Cullin-1 | A | protein | 813 | Homo sapiens | Q13616 (AlphaFold model) |
| E3 ubiquitin-protein ligase RBX1 | B | protein | 108 | Homo sapiens | P62877 (AlphaFold model) |
| Cullin-associated NEDD8-dissociated protein 1 | C | protein | 1238 | Homo sapiens | Q86VP6 (AlphaFold model) |
| DCN1-like protein 1 | F | protein | 261 | Homo sapiens | Q96GG9 (AlphaFold model) |
>8OR2_1 Cullin-1 (chains A) MWSHPQFEKGSAGSAAGSGAGWSHPQFEKLEVLFQGPMSSTRSQNPHGLKQIGLDQIWDD LRAGIQQVYTRQSMAKSRYMELYTHVYNYCTSVHQSNQARGAGVPPSKSKKGQTPGGAQF VGLELYKRLKEFLKNYLTNLLKDGEDLMDESVLKFYTQQWEDYRFSSKVLNGICAYLNRH WVRRECDEGRKGIYEIYSLALVTWRDCLFRPLNKQVTNAVLKLIEKERNGETINTRLISG VVQSYVELGLNEDDAFAKGPTLTVYKESFESQFLADTERFYTRESTEFLQQNPVTEYMKK AEARLLEEQRRVQVYLHESTQDELARKCEQVLIEKHLEIFHTEFQNLLDADKNEDLGRMY NLVSRIQDGLGELKKLLETHIHNQGLAAIEKCGEAALNDPKMYVQTVLDVHKKYNALVMS AFNNDAGFVAALDKACGRFINNNAVTKMAQSSSKSPELLARYCDSLLKKSSKNPEEAELE DTLNQVMVVFKYIEDKDVFQKFYAKMLAKRLVHQNSASDDAEASMISKLKQACGFEYTSK LQRMFQDIGVSKDLNEQFKKHLTNSEPLDLDFSIQVLSSGSWPFQQSCTFALPSELERSY QRFTAFYASRHSGRKLTWLYQLSKGELVTNCFKNRYTLQASTFQMAILLQYNTEDAYTVQ QLTDSTQIKMDILAQVLQILLKSKLLVLEDENANVDEVELKPDTLIKLYLGYKNKKLRVN INVPMKTEQKQEQETTHKNIEEDRKLLIQAAIVRIMKMRKVLKHQQLLGEVLTQLSSRFK PRVPVIKKCIDILIEKEYLERVDGEKDTYSYLA
>8OR2_2 E3 ubiquitin-protein ligase RBX1 (chains B) MAAAMDVDTPSGTNSGAGKKRFEVKKWNAVALWAWDIVVDNCAICRNHIMDLCIECQANQ ASATSEECTVAWGVCNHAFHFHCISRWLKTRQVCPLDNREWEFQKYGH
>8OR2_3 Cullin-associated NEDD8-dissociated protein 1 (chains C) GSPEFPGRMASASYHISNLLEKMTSSDKDFRFMATNDLMTELQKDSIKLDDDSERKVVKM ILKLLEDKNGEVQNLAVKCLGPLVSKVKEYQVETIVDTLCTNMLSDKEQLRDISSIGLKT VIGELPPASSGSALAANVCKKITGRLTSAIAKQEDVSVQLEALDIMADMLSRQGGLLVNF HPSILTCLLPQLTSPRLAVRKRTIIALGHLVMSCGNIVFVDLIEHLLSELSKNDSMSTTR TYIQCIAAISRQAGHRIGEYLEKIIPLVVKFCNVDDDELREYCIQAFESFVRRCPKEVYP HVSTIINICLKYLTYDPNYNYDDEDEDENAMDADGGDDDDQGSDDEYSDDDDMSWKVRRA AAKCLDAVVSTRHEMLPEFYKTVSPALISRFKEREENVKADVFHAYLSLLKQTRPVQSWL CDPDAMEQGETPLTMLQSQVPNIVKALHKQMKEKSVKTRQCCFNMLTELVNVLPGALTQH IPVLVPGIIFSLNDKSSSSNLKIDALSCLYVILCNHSPQVFHPHVQALVPPVVACVGDPF YKITSEALLVTQQLVKVIRPLDQPSSFDATPYIKDLFTCTIKRLKAADIDQEVKERAISC MGQIICNLGDNLGSDLPNTLQIFLERLKNEITRLTTVKALTLIAGSPLKIDLRPVLGEGV PILASFLRKNQRALKLGTLSALDILIKNYSDSLTAAMIDAVLDELPPLISESDMHVSQMA ISFLTTLAKVYPSSLSKISGSILNELIGLVRSPLLQGGALSAMLDFFQALVVTGTNNLGY MDLLRMLTGPVYSQSTALTHKQSYYSIAKCVAALTRACPKEGPAVVGQFIQDVKNSRSTD SIRLLALLSLGEVGHHIDLSGQLELKSVILEAFSSPSEEVKSAASYALGSISVGNLPEYL PFVLQEITSQPKRQYLLLHSLKEIISSASVVGLKPYVENIWALLLKHCECAEEGTRNVVA ECLGKLTLIDPETLLPRLKGYLISGSSYARSSVVTAVKFTISDHPQPIDPLLKNCIGDFL KTLEDPDLNVRRVALVTFNSAAHNKPSLIRDLLDTVLPHLYNETKVRKELIREVEMGPFK HTVDDGLDIRKAAFECMYTLLDSCLDRLDIFEFLNHVEDGLKDHYDIKMLTFLMLVRLST LCPSAVLQRLDRLVEPLRATCTTKVKANSVKQEFEKQDELKRSAMRAVAALLTIPEAEKS PLMSEFQSQISSNPELAAIFESIQKDSSSTNLESMDTS
>8OR2_4 DCN1-like protein 1 (chains F) GSMNKLKSSQKDKVRQFMIFTQSSEKTAVSCLSQNDWKLDVATDNFFQNPELYIRESVKG SLDRKKLEQLYNRYKDPQDENKIGIDGIQQFCDDLALDPASISVLIIAWKFRAATQCEFS KQEFMDGMTELGCDSIEKLKAQIPKMEQELKEPGRFKDFYQFTFNFAKNPGQKGLDLEMA IAYWNLVLNGRFKFLDLWNKFLLEHHKRSIPKDTWNLLLDFSTMIADDMSNYDEEGAWPV LIDDFVEFARPQIAGTKSTTV
| ID | Name | Formula | Copies |
|---|---|---|---|
| ZN | Zinc ion | Zn | 3 |
Structural and mechanistic insights into the CAND1-mediated SCF substrate receptor exchange. Shaaban, M., Clapperton, J.A., Ding, S. et al. Mol Cell (2023) 83:2332. DOI 10.1016/j.molcel.2023.05.034 · PubMed
Other PDB entries of the same protein (UniProt Q13616 (AlphaFold model), which also has an AlphaFold model), best resolution first:
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