8OR4: Cullin-1
Partially dissociated CAND1-CUL1-RBX1-SKP1-SKP2-CKS1-CDK2. Determined by electron microscopy at 3.8 Å resolution. Released 28 Jun 2023.
- Method
- Electron microscopy
- Resolution
- 3.8 Å
- Organism
- Homo sapiens
- Chains
- 7
- Atoms
- 15,036
- Mol. weight
- 353.26 kDa
- Released
- 28 Jun 2023
Explore 8OR4 in 3D
Show helices and sheets
RCSB PDB
PDBe
Secondary structure: helices and β-sheets
8OR4 contains 109 α-helices and 15 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: 37 helices, 3 β-strands
| Element | Residues | Length | Sheet |
|---|
| α-helix | 24-31 | 8 | |
| α-helix | 40-42 | 3 | |
| α-helix | 43-52 | 10 | |
| α-helix | 88-106 | 19 | |
| α-helix | 116-136 | 21 | |
| α-helix | 138-143 | 6 | |
| α-helix | 159-171 | 13 | |
| α-helix | 175-192 | 18 | |
| α-helix | 199-210 | 12 | |
| α-helix | 226-228 | 3 | |
| α-helix | 229-233 | 5 | |
| α-helix | 234-254 | 21 | |
| α-helix | 258-278 | 21 | |
| α-helix | 281-283 | 3 | |
| α-helix | 284-295 | 12 | |
| α-helix | 297-299 | 3 | |
| α-helix | 300-312 | 13 | |
| α-helix | 316-326 | 11 | |
| α-helix | 333-355 | 23 | |
| α-helix | 357-361 | 5 | |
| α-helix | 363-384 | 22 | |
| α-helix | 389-404 | 16 | |
| α-helix | 407-411 | 5 | |
| α-helix | 417-429 | 13 | |
| α-helix | 442-455 | 14 | |
| α-helix | 460-475 | 16 | |
| α-helix | 482-495 | 14 | |
| α-helix | 498-527 | 30 | |
| β-strand | 538-539 | 2 | 1 |
| α-helix | 557-564 | 8 | |
| α-helix | 569-572 | 4 | |
| β-strand | 601 | 1 | 2 |
| α-helix | 606-611 | 6 | |
| α-helix | 624-629 | 6 | |
| α-helix | 633-645 | 13 | |
| β-strand | 682 | 1 | 2 |
| α-helix | 686-688 | 3 | |
| α-helix | 689-721 | 33 | |
| α-helix | 728-736 | 9 | |
| α-helix | 746-758 | 13 | |
Chain B: 1 helix, 1 β-strand
| Element | Residues | Length | Sheet |
|---|
| β-strand | 30-31 | 2 | 1 |
| α-helix | 81-91 | 11 | |
Chain C: 51 helices, 0 β-strands
| Element | Residues | Length | Sheet |
|---|
| α-helix | 7-15 | 9 | |
| α-helix | 20-35 | 16 | |
| α-helix | 43-56 | 14 | |
| α-helix | 62-68 | 7 | |
| α-helix | 84-94 | 11 | |
| α-helix | 100-114 | 15 | |
| α-helix | 128-138 | 11 | |
| α-helix | 139-142 | 4 | |
| α-helix | 149-164 | 16 | |
| α-helix | 167-170 | 4 | |
| α-helix | 173-180 | 8 | |
| α-helix | 182-185 | 4 | |
| α-helix | 189-205 | 17 | |
| α-helix | 213-225 | 13 | |
| α-helix | 233-244 | 12 | |
| α-helix | 250-264 | 15 | |
| α-helix | 272-284 | 13 | |
| α-helix | 292-302 | 11 | |
| α-helix | 347-363 | 17 | |
| α-helix | 375-382 | 8 | |
| 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 | 514-527 | 14 | |
| α-helix | 533-548 | 16 | |
| α-helix | 562-576 | 15 | |
| α-helix | 583-600 | 18 | |
| α-helix | 603-605 | 3 | |
| α-helix | 608-620 | 13 | |
| α-helix | 626-634 | 9 | |
| α-helix | 645-649 | 5 | |
| α-helix | 652-656 | 5 | |
| α-helix | 667-676 | 10 | |
| α-helix | 684-686 | 3 | |
| α-helix | 691-694 | 4 | |
| α-helix | 698-700 | 3 | |
| α-helix | 703-719 | 17 | |
| α-helix | 736-742 | 7 | |
| α-helix | 759-761 | 3 | |
| α-helix | 764-767 | 4 | |
| α-helix | 790-805 | 16 | |
| α-helix | 811-813 | 3 | |
| α-helix | 815-818 | 4 | |
| α-helix | 828-835 | 8 | |
| α-helix | 870-876 | 7 | |
| α-helix | 884-886 | 3 | |
| α-helix | 911-916 | 6 | |
| α-helix | 929-932 | 4 | |
| α-helix | 949-952 | 4 | |
Chain D: 9 helices, 3 β-strands
| Element | Residues | Length | Sheet |
|---|
| β-strand | 4-7 | 4 | 3 |
| β-strand | 13-16 | 4 | 3 |
| α-helix | 21-23 | 3 | |
| α-helix | 25-32 | 8 | |
| β-strand | 46 | 1 | 3 |
| α-helix | 52-60 | 9 | |
| α-helix | 64-66 | 3 | |
| α-helix | 93-99 | 7 | |
| α-helix | 103-116 | 14 | |
| α-helix | 121-133 | 13 | |
| α-helix | 138-143 | 6 | |
| α-helix | 155-162 | 8 | |
Chain E: 8 helices, 8 β-strands
| Element | Residues | Length | Sheet |
|---|
| α-helix | 102-110 | 9 | |
| α-helix | 114-120 | 7 | |
| α-helix | 125-131 | 7 | |
| β-strand | 140-141 | 2 | 4 |
| α-helix | 149-158 | 10 | |
| β-strand | 170 | 1 | 5 |
| β-strand | 185-189 | 5 | 6 |
| β-strand | 193 | 1 | 5 |
| α-helix | 195-201 | 7 | |
| β-strand | 210-214 | 5 | 6 |
| α-helix | 220-222 | 3 | |
| α-helix | 224-228 | 5 | |
| α-helix | 252-254 | 3 | |
| β-strand | 409 | 1 | 7 |
| β-strand | 412 | 1 | 7 |
| β-strand | 416-417 | 2 | 4 |
Chain G: 1 helix, 0 β-strands
| Element | Residues | Length | Sheet |
|---|
| α-helix | 26-31 | 6 | |
Chain H: 2 helices, 0 β-strands
| Element | Residues | Length | Sheet |
|---|
| α-helix | 183-187 | 5 | |
| α-helix | 208-217 | 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
>8OR4_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
>8OR4_2 E3 ubiquitin-protein ligase RBX1 (chains B)
MAAAMDVDTPSGTNSGAGKKRFEVKKWNAVALWAWDIVVDNCAICRNHIMDLCIECQANQ
ASATSEECTVAWGVCNHAFHFHCISRWLKTRQVCPLDNREWEFQKYGH
Sequence of entity 3 (C), FASTA
>8OR4_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
>8OR4_4 S-phase kinase-associated protein 1 (chains D)
MPSIKLQSSDGEIFEVDVEIAKQSVTIKTMLEDLGMDDEGDDDPVPLPNVNAAILKKVIQ
WCTHHKDDPPPPEDDENKEKRTDDIPVWDQEFLKVDQGTLFELILAANYLDIKGLLDVTC
KTVANMIKGKTPEEIRKTFNIKNDFTEEEEAQVRKENQWCEEK
Sequence of entity 5 (E), FASTA
>8OR4_5 S-phase kinase-associated protein 2 (chains E)
GSPEFMHRKHLQEIPDLSSNVATSFTWGWDSSKTSELLSGMGVSALEKEEPDSENIPQEL
LSNLGHPESPPRKRLKSKGSDKDFVIVRRPKLNRENFPGVSWDSLPDELLLGIFSCLCLP
ELLKVSGVCKRWYRLASDESLWQTLDLTGKNLHPDVTGRLLSQGVIAFRCPRSFMDQPLA
EHFSPFRVQHMDLSNSVIEVSTLHGILSQCSKLQNLSLEGLRLSDPIVNTLAKNSNLVRL
NLSGCSGFSEFALQTLLSSCSRLDELNLSWCFDFTEKHVQVAVAHVSETITQLNLSGYRK
NLQKSDLSTLVRRCPNLVHLDLSDSVMLKNDCFQEFFQLNYLQHLSLSRCYDIIPETLLE
LGEIPTLKTLQVFGIVPDGTLQLLKEALPHLQINCSHFTTIARPTIGNKKNQEIWGIKCR
LTLQKPSCL
Sequence of entity 6 (G), FASTA
>8OR4_6 Cyclin-dependent kinases regulatory subunit 1 (chains G)
GPLGSQIYYSDKYDDEEFEYRHVMLPKDIAKLVPKTHLMSESEWRNLGVQQSQGWVHYMI
HEPEPHILLFRRPL
Sequence of entity 7 (H), FASTA
>8OR4_7 Cyclin-dependent kinase 2 (chains H)
MENFQKVEKIGEGTYGVVYKARNKLTGEVVALKKIRLDTETEGVPSTAIREISLLKELNH
PNIVKLLDVIHTENKLYLVFEFLHQDLKKFMDASALTGIPLPLIKSYLFQLLQGLAFCHS
HRVLHRDLKPQNLLINTEGAIKLADFGLARAFGVPVRTYTHEVVTLWYRAPEILLGCKYY
STAVDIWSLGCIFAEMVTRRALFPGDSEIDQLFRIFRTLGTPDEVVWPGVTSMPDYKPSF
PKWARQDFSKVVPPLDEDGRSLLSQMLHYDPNKRISAKAALAHPFFQDVTKPVPHLRL
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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