8OR0: CAND1-CUL1-RBX1-SKP1-SKP2-CKS1-CDK2
CAND1-CUL1-RBX1-SKP1-SKP2-CKS1-CDK2. Determined by electron microscopy at 3.1 Å resolution. Released 28 Jun 2023.
- Method
- Electron microscopy
- Resolution
- 3.1 Å
- Organism
- Homo sapiens
- Chains
- 7
- Atoms
- 18,823
- Mol. weight
- 353.46 kDa
- Ligands
- ZN
- Released
- 28 Jun 2023
Explore 8OR0 in 3D
Show helices and sheets
RCSB PDB
PDBe
Secondary structure: helices and β-sheets
8OR0 contains 128 α-helices and 37 β-strands across 7 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: 34 helices, 10 β-strands
| Element | Residues | Length | Sheet |
|---|
| α-helix | 19-32 | 14 | |
| α-helix | 40-51 | 12 | |
| α-helix | 89-105 | 17 | |
| α-helix | 115-136 | 22 | |
| α-helix | 159-170 | 12 | |
| α-helix | 175-191 | 17 | |
| α-helix | 199-210 | 12 | |
| α-helix | 227 | 1 | |
| α-helix | 228-233 | 6 | |
| α-helix | 234-254 | 21 | |
| α-helix | 257-277 | 21 | |
| α-helix | 284-297 | 14 | |
| α-helix | 300-312 | 13 | |
| α-helix | 316-326 | 11 | |
| α-helix | 334-354 | 21 | |
| α-helix | 363-380 | 18 | |
| α-helix | 381-385 | 5 | |
| α-helix | 389-404 | 16 | |
| α-helix | 407-412 | 6 | |
| α-helix | 418-430 | 13 | |
| α-helix | 443-453 | 11 | |
| α-helix | 459-475 | 17 | |
| α-helix | 482-495 | 14 | |
| α-helix | 498-524 | 27 | |
| β-strand | 537-541 | 5 | 1 |
| α-helix | 548-550 | 3 | |
| α-helix | 554-556 | 3 | |
| α-helix | 560-573 | 14 | |
| β-strand | 577-579 | 3 | 1 |
| β-strand | 582 | 1 | 1 |
| β-strand | 590-592 | 3 | 2 |
| β-strand | 600 | 1 | 3 |
| α-helix | 605-612 | 8 | |
| α-helix | 622-629 | 8 | |
| α-helix | 633-644 | 12 | |
| β-strand | 681 | 1 | 3 |
| α-helix | 691-718 | 28 | |
| β-strand | 726 | 1 | 4 |
| α-helix | 727-737 | 11 | |
| α-helix | 746-756 | 11 | |
| α-helix | 757-761 | 5 | |
| β-strand | 762-764 | 3 | 5 |
| β-strand | 771 | 1 | 4 |
| β-strand | 772-774 | 3 | 5 |
Chain B: 5 helices, 8 β-strands
| Element | Residues | Length | Sheet |
|---|
| β-strand | 22-24 | 3 | 2 |
| β-strand | 29-35 | 7 | 1 |
| α-helix | 36-40 | 5 | |
| β-strand | 42 | 1 | 6 |
| β-strand | 47 | 1 | 6 |
| α-helix | 52-53 | 2 | |
| α-helix | 54-58 | 5 | |
| α-helix | 64-67 | 4 | |
| β-strand | 70 | 1 | 7 |
| β-strand | 80 | 1 | 7 |
| α-helix | 81-87 | 7 | |
| β-strand | 93 | 1 | 8 |
| β-strand | 100 | 1 | 8 |
Chain C: 65 helices, 2 β-strands
| Element | Residues | Length | Sheet |
|---|
| α-helix | 5-15 | 11 | |
| α-helix | 21-35 | 15 | |
| α-helix | 44-57 | 14 | |
| α-helix | 62-78 | 17 | |
| α-helix | 84-95 | 12 | |
| α-helix | 100-116 | 17 | |
| α-helix | 129-141 | 13 | |
| α-helix | 149-164 | 16 | |
| α-helix | 173-180 | 8 | |
| α-helix | 182-185 | 4 | |
| α-helix | 189-205 | 17 | |
| α-helix | 214-226 | 13 | |
| α-helix | 232-244 | 13 | |
| α-helix | 253-264 | 12 | |
| α-helix | 271-284 | 14 | |
| α-helix | 291-301 | 11 | |
| α-helix | 346-363 | 18 | |
| α-helix | 368-373 | 6 | |
| α-helix | 376-382 | 7 | |
| α-helix | 388-404 | 17 | |
| α-helix | 424-442 | 19 | |
| α-helix | 448-464 | 17 | |
| α-helix | 473-485 | 13 | |
| α-helix | 491-507 | 17 | |
| α-helix | 510-512 | 3 | |
| α-helix | 517-528 | 12 | |
| α-helix | 533-550 | 18 | |
| α-helix | 562-574 | 13 | |
| α-helix | 583-600 | 18 | |
| α-helix | 608-611 | 4 | |
| α-helix | 613-620 | 8 | |
| α-helix | 626-636 | 11 | |
| α-helix | 645-657 | 13 | |
| α-helix | 664-680 | 17 | |
| α-helix | 687-695 | 9 | |
| α-helix | 707-722 | 16 | |
| α-helix | 734-742 | 9 | |
| α-helix | 750-764 | 15 | |
| α-helix | 772-784 | 13 | |
| α-helix | 793-808 | 16 | |
| α-helix | 815-825 | 11 | |
| α-helix | 832-845 | 14 | |
| α-helix | 858-865 | 8 | |
| α-helix | 871-886 | 16 | |
| α-helix | 888-901 | 14 | |
| α-helix | 907-919 | 13 | |
| α-helix | 922-925 | 4 | |
| α-helix | 929-936 | 8 | |
| α-helix | 937-940 | 4 | |
| α-helix | 945-958 | 14 | |
| α-helix | 963-970 | 8 | |
| α-helix | 973-976 | 4 | |
| α-helix | 979-989 | 11 | |
| α-helix | 1001-1014 | 14 | |
| α-helix | 1020-1036 | 17 | |
| α-helix | 1038-1041 | 4 | |
| α-helix | 1045-1054 | 10 | |
| β-strand | 1064 | 1 | 9 |
| β-strand | 1075 | 1 | 9 |
| α-helix | 1079-1095 | 17 | |
| α-helix | 1102-1111 | 10 | |
| α-helix | 1117-1132 | 16 | |
| α-helix | 1135-1137 | 3 | |
| α-helix | 1142-1153 | 12 | |
| α-helix | 1157-1158 | 2 | |
| α-helix | 1164-1184 | 21 | |
| α-helix | 1205-1209 | 5 | |
Chain D: 7 helices, 3 β-strands
| Element | Residues | Length | Sheet |
|---|
| β-strand | 3-7 | 5 | 10 |
| β-strand | 13-17 | 5 | 10 |
| α-helix | 28-31 | 4 | |
| β-strand | 46 | 1 | 10 |
| α-helix | 52-64 | 13 | |
| α-helix | 94-98 | 5 | |
| α-helix | 103-115 | 13 | |
| α-helix | 120-132 | 13 | |
| α-helix | 138-145 | 8 | |
| α-helix | 156-161 | 6 | |
Chain E: 13 helices, 12 β-strands
| Element | Residues | Length | Sheet |
|---|
| α-helix | 102-109 | 8 | |
| α-helix | 114-119 | 6 | |
| α-helix | 125-131 | 7 | |
| β-strand | 139-141 | 3 | 11 |
| α-helix | 149-156 | 8 | |
| β-strand | 162-164 | 3 | 11 |
| β-strand | 169-170 | 2 | 12 |
| β-strand | 185-187 | 3 | 11 |
| β-strand | 192-193 | 2 | 12 |
| α-helix | 196-198 | 3 | |
| β-strand | 213-214 | 2 | 13 |
| α-helix | 220-226 | 7 | |
| β-strand | 236 | 1 | 14 |
| β-strand | 237-238 | 2 | 13 |
| α-helix | 245-254 | 10 | |
| β-strand | 261-264 | 4 | 14 |
| α-helix | 272-275 | 4 | |
| α-helix | 276-279 | 4 | |
| β-strand | 287-291 | 5 | 14 |
| α-helix | 299-308 | 10 | |
| β-strand | 314-315 | 2 | 14 |
| α-helix | 327-330 | 4 | |
| α-helix | 353-355 | 3 | |
| α-helix | 378-382 | 5 | |
| β-strand | 416-417 | 2 | 11 |
Chain G: 1 helix, 2 β-strands
| Element | Residues | Length | Sheet |
|---|
| β-strand | 22 | 1 | 15 |
| α-helix | 28-30 | 3 | |
| β-strand | 67 | 1 | 15 |
Chain H: 3 helices, 0 β-strands
| Element | Residues | Length | Sheet |
|---|
| α-helix | 171-174 | 4 | |
| α-helix | 183-186 | 4 | |
| α-helix | 210-219 | 10 | |
Molecules and chains
| 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) |
| S-phase kinase-associated protein 1 | D | protein | 163 | Homo sapiens | P63208 (AlphaFold model) |
| S-phase kinase-associated protein 2 | E | protein | 429 | Homo sapiens | Q13309 |
| Cyclin-dependent kinases regulatory subunit 1 | G | protein | 74 | Homo sapiens | P61024 |
| Cyclin-dependent kinase 2 | H | protein | 298 | Homo sapiens | P24941 |
Sequence of entity 1 (A), FASTA
>8OR0_1 Cullin-1 (chains A)
MWSHPQFEKGSAGSAAGSGAGWSHPQFEKLEVLFQGPMSSTRSQNPHGLKQIGLDQIWDD
LRAGIQQVYTRQSMAKSRYMELYTHVYNYCTSVHQSNQARGAGVPPSKSKKGQTPGGAQF
VGLELYKRLKEFLKNYLTNLLKDGEDLMDESVLKFYTQQWEDYRFSSKVLNGICAYLNRH
WVRRECDEGRKGIYEIYSLALVTWRDCLFRPLNKQVTNAVLKLIEKERNGETINTRLISG
VVQSYVELGLNEDDAFAKGPTLTVYKESFESQFLADTERFYTRESTEFLQQNPVTEYMKK
AEARLLEEQRRVQVYLHESTQDELARKCEQVLIEKHLEIFHTEFQNLLDADKNEDLGRMY
NLVSRIQDGLGELKKLLETHIHNQGLAAIEKCGEAALNDPKMYVQTVLDVHKKYNALVMS
AFNNDAGFVAALDKACGRFINNNAVTKMAQSSSKSPELLARYCDSLLKKSSKNPEEAELE
DTLNQVMVVFKYIEDKDVFQKFYAKMLAKRLVHQNSASDDAEASMISKLKQACGFEYTSK
LQRMFQDIGVSKDLNEQFKKHLTNSEPLDLDFSIQVLSSGSWPFQQSCTFALPSELERSY
QRFTAFYASRHSGRKLTWLYQLSKGELVTNCFKNRYTLQASTFQMAILLQYNTEDAYTVQ
QLTDSTQIKMDILAQVLQILLKSKLLVLEDENANVDEVELKPDTLIKLYLGYKNKKLRVN
INVPMKTEQKQEQETTHKNIEEDRKLLIQAAIVRIMKMRKVLKHQQLLGEVLTQLSSRFK
PRVPVIKKCIDILIEKEYLERVDGEKDTYSYLA
Sequence of entity 2 (B), FASTA
>8OR0_2 E3 ubiquitin-protein ligase RBX1 (chains B)
MAAAMDVDTPSGTNSGAGKKRFEVKKWNAVALWAWDIVVDNCAICRNHIMDLCIECQANQ
ASATSEECTVAWGVCNHAFHFHCISRWLKTRQVCPLDNREWEFQKYGH
Sequence of entity 3 (C), FASTA
>8OR0_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
Sequence of entity 4 (D), FASTA
>8OR0_4 S-phase kinase-associated protein 1 (chains D)
MPSIKLQSSDGEIFEVDVEIAKQSVTIKTMLEDLGMDDEGDDDPVPLPNVNAAILKKVIQ
WCTHHKDDPPPPEDDENKEKRTDDIPVWDQEFLKVDQGTLFELILAANYLDIKGLLDVTC
KTVANMIKGKTPEEIRKTFNIKNDFTEEEEAQVRKENQWCEEK
Sequence of entity 5 (E), FASTA
>8OR0_5 S-phase kinase-associated protein 2 (chains E)
GSPEFMHRKHLQEIPDLSSNVATSFTWGWDSSKTSELLSGMGVSALEKEEPDSENIPQEL
LSNLGHPESPPRKRLKSKGSDKDFVIVRRPKLNRENFPGVSWDSLPDELLLGIFSCLCLP
ELLKVSGVCKRWYRLASDESLWQTLDLTGKNLHPDVTGRLLSQGVIAFRCPRSFMDQPLA
EHFSPFRVQHMDLSNSVIEVSTLHGILSQCSKLQNLSLEGLRLSDPIVNTLAKNSNLVRL
NLSGCSGFSEFALQTLLSSCSRLDELNLSWCFDFTEKHVQVAVAHVSETITQLNLSGYRK
NLQKSDLSTLVRRCPNLVHLDLSDSVMLKNDCFQEFFQLNYLQHLSLSRCYDIIPETLLE
LGEIPTLKTLQVFGIVPDGTLQLLKEALPHLQINCSHFTTIARPTIGNKKNQEIWGIKCR
LTLQKPSCL
Sequence of entity 6 (G), FASTA
>8OR0_6 Cyclin-dependent kinases regulatory subunit 1 (chains G)
GPLGSQIYYSDKYDDEEFEYRHVMLPKDIAKLVPKTHLMSESEWRNLGVQQSQGWVHYMI
HEPEPHILLFRRPL
Sequence of entity 7 (H), FASTA
>8OR0_7 Cyclin-dependent kinase 2 (chains H)
MENFQKVEKIGEGTYGVVYKARNKLTGEVVALKKIRLDTETEGVPSTAIREISLLKELNH
PNIVKLLDVIHTENKLYLVFEFLHQDLKKFMDASALTGIPLPLIKSYLFQLLQGLAFCHS
HRVLHRDLKPQNLLINTEGAIKLADFGLARAFGVPVRTYTHEVVTLWYRAPEILLGCKYY
STAVDIWSLGCIFAEMVTRRALFPGDSEIDQLFRIFRTLGTPDEVVWPGVTSMPDYKPSF
PKWARQDFSKVVPPLDEDGRSLLSQMLHYDPNKRISAKAALAHPFFQDVTKPVPHLRL
Ligands and cofactors
| ID | Name | Formula | Copies |
|---|
| ZN | Zinc ion | Zn | 3 |
Primary citation
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:
- 3TDU 1.5 Å, N-terminal acetylation acts as an avidity enhancer within an interconnected multiprotein…
- 5V89 1.55 Å, Structure of DCN4 PONY domain bound to CUL1 WHB
- 3TDZ 2.0 Å, N-terminal acetylation acts as an avidity enhancer within an interconnected multiprotein…
- 8CAF 2.66 Å, N8C_Fab3b in complex with NEDD8-CUL1(WHB)
- 7Z8R 2.7 Å, CAND1-CUL1-RBX1
- 7Z8V 2.7 Å, CAND1-SCF-SKP2 (SKP1deldel) CAND1 engaged SCF rocked
- 8OR3 2.9 Å, CAND1-CUL1-RBX1-SKP1-SKP2-DCNL1
- 9QO4 2.95 Å, Dissociation-state-3 of 9-subunit CSN and SCF (SKP1-SKP2-CKS1) complex
- 1LDJ 3.0 Å, Structure of the Cul1-Rbx1-Skp1-F boxSkp2 SCF Ubiquitin Ligase Complex
- 4F52 3.0 Å, Structure of a Glomulin-RBX1-CUL1 complex
- 7Z8T 3.0 Å, CAND1-SCF-SKP2 CAND1 engaged SCF rocked
- 9XZL 3.0 Å, Cryo-EM structure of F-box helicase 1 (FBH1) bound to an SCF ubiquitin ligase complex…
Browse structure collections
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