8OR3: CAND1-CUL1-RBX1-SKP1-SKP2-DCNL1
CAND1-CUL1-RBX1-SKP1-SKP2-DCNL1. Determined by electron microscopy at 2.9 Å resolution. Released 28 Jun 2023.
- Method
- Electron microscopy
- Resolution
- 2.9 Å
- Organism
- Homo sapiens
- Chains
- 6
- Atoms
- 18,710
- Mol. weight
- 340.89 kDa
- Ligands
- ZN
- Released
- 28 Jun 2023
Explore 8OR3 in 3D
Show helices and sheets
RCSB PDB
PDBe
Secondary structure: helices and β-sheets
8OR3 contains 132 α-helices and 29 β-strands across 6 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, 14 β-strands
| Element | Residues | Length | Sheet |
|---|
| α-helix | 26-31 | 6 | |
| β-strand | 37 | 1 | 1 |
| α-helix | 40-53 | 14 | |
| α-helix | 88-106 | 19 | |
| α-helix | 115-136 | 22 | |
| α-helix | 140-142 | 3 | |
| α-helix | 159-169 | 11 | |
| α-helix | 174-192 | 19 | |
| 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 | 282-295 | 14 | |
| α-helix | 297-299 | 3 | |
| α-helix | 300-312 | 13 | |
| α-helix | 316-327 | 12 | |
| α-helix | 334-354 | 21 | |
| α-helix | 363-384 | 22 | |
| α-helix | 389-404 | 16 | |
| α-helix | 407-412 | 6 | |
| α-helix | 417-430 | 14 | |
| β-strand | 431 | 1 | 2 |
| α-helix | 443-453 | 11 | |
| α-helix | 459-475 | 17 | |
| β-strand | 479 | 1 | 2 |
| α-helix | 482-495 | 14 | |
| α-helix | 498-524 | 27 | |
| β-strand | 535-541 | 7 | 3 |
| α-helix | 542-544 | 3 | |
| α-helix | 554-556 | 3 | |
| α-helix | 560-573 | 14 | |
| β-strand | 577-582 | 6 | 3 |
| β-strand | 587-592 | 6 | 3 |
| β-strand | 599-604 | 6 | 3 |
| α-helix | 605-612 | 8 | |
| β-strand | 615 | 1 | 4 |
| α-helix | 622-629 | 8 | |
| α-helix | 633-644 | 12 | |
| β-strand | 649 | 1 | 5 |
| β-strand | 671 | 1 | 5 |
| β-strand | 681-683 | 3 | 3 |
| α-helix | 691-721 | 31 | |
| β-strand | 724-726 | 3 | 6 |
| α-helix | 727-738 | 12 | |
| α-helix | 746-758 | 13 | |
| β-strand | 762-764 | 3 | 6 |
| β-strand | 771-774 | 4 | 6 |
Chain B: 4 helices, 7 β-strands
| Element | Residues | Length | Sheet |
|---|
| β-strand | 20 | 1 | 4 |
| β-strand | 23-35 | 13 | 3 |
| α-helix | 36-39 | 4 | |
| β-strand | 41 | 1 | 7 |
| β-strand | 48 | 1 | 7 |
| α-helix | 54-58 | 5 | |
| α-helix | 63-65 | 3 | |
| β-strand | 70-73 | 4 | 8 |
| β-strand | 78-80 | 3 | 8 |
| α-helix | 81-87 | 7 | |
| β-strand | 103-105 | 3 | 8 |
Chain C: 69 helices, 2 β-strands
| Element | Residues | Length | Sheet |
|---|
| α-helix | 5-14 | 10 | |
| α-helix | 20-35 | 16 | |
| α-helix | 43-56 | 14 | |
| α-helix | 62-75 | 14 | |
| α-helix | 76-78 | 3 | |
| α-helix | 81-95 | 15 | |
| α-helix | 100-116 | 17 | |
| α-helix | 129-142 | 14 | |
| α-helix | 148-164 | 17 | |
| α-helix | 173-180 | 8 | |
| α-helix | 181-185 | 5 | |
| α-helix | 189-205 | 17 | |
| α-helix | 214-226 | 13 | |
| α-helix | 232-244 | 13 | |
| α-helix | 248-255 | 8 | |
| α-helix | 257-262 | 6 | |
| α-helix | 263-265 | 3 | |
| α-helix | 271-284 | 14 | |
| α-helix | 291-302 | 12 | |
| α-helix | 348-363 | 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 | 510-513 | 4 | |
| α-helix | 517-519 | 3 | |
| α-helix | 521-528 | 8 | |
| α-helix | 533-550 | 18 | |
| α-helix | 562-564 | 3 | |
| α-helix | 565-576 | 12 | |
| α-helix | 583-600 | 18 | |
| α-helix | 607-620 | 14 | |
| α-helix | 625-636 | 12 | |
| α-helix | 645-657 | 13 | |
| α-helix | 664-680 | 17 | |
| α-helix | 687-694 | 8 | |
| α-helix | 697-700 | 4 | |
| α-helix | 706-722 | 17 | |
| α-helix | 724-726 | 3 | |
| α-helix | 733-742 | 10 | |
| α-helix | 750-765 | 16 | |
| α-helix | 772-784 | 13 | |
| α-helix | 793-809 | 17 | |
| α-helix | 814-825 | 12 | |
| α-helix | 832-846 | 15 | |
| α-helix | 857-865 | 9 | |
| α-helix | 870-880 | 11 | |
| α-helix | 882-886 | 5 | |
| α-helix | 888-901 | 14 | |
| α-helix | 906-919 | 14 | |
| α-helix | 922-925 | 4 | |
| α-helix | 929-938 | 10 | |
| α-helix | 945-960 | 16 | |
| α-helix | 963-972 | 10 | |
| α-helix | 979-990 | 12 | |
| α-helix | 1001-1009 | 9 | |
| α-helix | 1010-1014 | 5 | |
| α-helix | 1020-1036 | 17 | |
| α-helix | 1045-1055 | 11 | |
| β-strand | 1063-1068 | 6 | 1 |
| β-strand | 1071-1076 | 6 | 1 |
| α-helix | 1079-1095 | 17 | |
| α-helix | 1102-1113 | 12 | |
| α-helix | 1117-1132 | 16 | |
| α-helix | 1135-1140 | 6 | |
| α-helix | 1147-1152 | 6 | |
| α-helix | 1163-1183 | 21 | |
| α-helix | 1204-1209 | 6 | |
Chain D: 7 helices, 2 β-strands
| Element | Residues | Length | Sheet |
|---|
| β-strand | 3-6 | 4 | 9 |
| β-strand | 14-17 | 4 | 9 |
| α-helix | 25-29 | 5 | |
| α-helix | 52-64 | 13 | |
| α-helix | 97-99 | 3 | |
| α-helix | 104-116 | 13 | |
| α-helix | 119-133 | 15 | |
| α-helix | 138-145 | 8 | |
| α-helix | 154-160 | 7 | |
Chain E: 7 helices, 2 β-strands
| Element | Residues | Length | Sheet |
|---|
| α-helix | 102-109 | 8 | |
| α-helix | 114-120 | 7 | |
| α-helix | 125-130 | 6 | |
| α-helix | 149-156 | 8 | |
| β-strand | 160 | 1 | 10 |
| β-strand | 183 | 1 | 10 |
| α-helix | 195 | 1 | |
| α-helix | 196-200 | 5 | |
| α-helix | 220-227 | 8 | |
Chain F: 11 helices, 2 β-strands
| Element | Residues | Length | Sheet |
|---|
| α-helix | 66-72 | 7 | |
| α-helix | 87-90 | 4 | |
| α-helix | 100-108 | 9 | |
| α-helix | 134-148 | 15 | |
| α-helix | 153-164 | 12 | |
| β-strand | 173 | 1 | 11 |
| α-helix | 175-185 | 11 | |
| α-helix | 193-198 | 6 | |
| α-helix | 207 | 1 | |
| β-strand | 208 | 1 | 11 |
| α-helix | 209 | 1 | |
| α-helix | 210-222 | 13 | |
| α-helix | 238-247 | 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 |
| DCN1-like protein 1 | F | protein | 261 | Homo sapiens | Q96GG9 |
Sequence of entity 1 (A), FASTA
>8OR3_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
>8OR3_2 E3 ubiquitin-protein ligase RBX1 (chains B)
MAAAMDVDTPSGTNSGAGKKRFEVKKWNAVALWAWDIVVDNCAICRNHIMDLCIECQANQ
ASATSEECTVAWGVCNHAFHFHCISRWLKTRQVCPLDNREWEFQKYGH
Sequence of entity 3 (C), FASTA
>8OR3_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
>8OR3_4 S-phase kinase-associated protein 1 (chains D)
MPSIKLQSSDGEIFEVDVEIAKQSVTIKTMLEDLGMDDEGDDDPVPLPNVNAAILKKVIQ
WCTHHKDDPPPPEDDENKEKRTDDIPVWDQEFLKVDQGTLFELILAANYLDIKGLLDVTC
KTVANMIKGKTPEEIRKTFNIKNDFTEEEEAQVRKENQWCEEK
Sequence of entity 5 (E), FASTA
>8OR3_5 S-phase kinase-associated protein 2 (chains E)
GSPEFMHRKHLQEIPDLSSNVATSFTWGWDSSKTSELLSGMGVSALEKEEPDSENIPQEL
LSNLGHPESPPRKRLKSKGSDKDFVIVRRPKLNRENFPGVSWDSLPDELLLGIFSCLCLP
ELLKVSGVCKRWYRLASDESLWQTLDLTGKNLHPDVTGRLLSQGVIAFRCPRSFMDQPLA
EHFSPFRVQHMDLSNSVIEVSTLHGILSQCSKLQNLSLEGLRLSDPIVNTLAKNSNLVRL
NLSGCSGFSEFALQTLLSSCSRLDELNLSWCFDFTEKHVQVAVAHVSETITQLNLSGYRK
NLQKSDLSTLVRRCPNLVHLDLSDSVMLKNDCFQEFFQLNYLQHLSLSRCYDIIPETLLE
LGEIPTLKTLQVFGIVPDGTLQLLKEALPHLQINCSHFTTIARPTIGNKKNQEIWGIKCR
LTLQKPSCL
Sequence of entity 6 (F), FASTA
>8OR3_6 DCN1-like protein 1 (chains F)
GSMNKLKSSQKDKVRQFMIFTQSSEKTAVSCLSQNDWKLDVATDNFFQNPELYIRESVKG
SLDRKKLEQLYNRYKDPQDENKIGIDGIQQFCDDLALDPASISVLIIAWKFRAATQCEFS
KQEFMDGMTELGCDSIEKLKAQIPKMEQELKEPGRFKDFYQFTFNFAKNPGQKGLDLEMA
IAYWNLVLNGRFKFLDLWNKFLLEHHKRSIPKDTWNLLLDFSTMIADDMSNYDEEGAWPV
LIDDFVEFARPQIAGTKSTTV
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
- 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…
- 9EFV 3.03 Å, Cryo-EM structure of CSN-N8CUL1 in complex with CSN5i-3
Browse structure collections
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