Crystal Structure of The Cand1-Cul1-Roc1 Complex. Determined by X-ray diffraction at 3.1 Å resolution. Released 14 Dec 2004.
Explore 1U6G in 3D Show helices and sheets RCSB PDB PDBe
1U6G contains 115 α-helices and 21 β-strands across 3 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 | 18-31 | 14 | |
| α-helix | 39-53 | 15 | |
| α-helix | 87-105 | 19 | |
| α-helix | 114-136 | 23 | |
| α-helix | 138-142 | 5 | |
| α-helix | 158-171 | 14 | |
| α-helix | 175-177 | 3 | |
| α-helix | 179-191 | 13 | |
| α-helix | 199-210 | 12 | |
| α-helix | 225-227 | 3 | |
| α-helix | 228-232 | 5 | |
| α-helix | 233-253 | 21 | |
| α-helix | 256-275 | 20 | |
| α-helix | 280-282 | 3 | |
| α-helix | 283-294 | 12 | |
| α-helix | 299-311 | 13 | |
| α-helix | 317-325 | 9 | |
| α-helix | 333-352 | 20 | |
| α-helix | 357-360 | 4 | |
| α-helix | 362-381 | 20 | |
| α-helix | 388-403 | 16 | |
| α-helix | 406-410 | 5 | |
| α-helix | 416-429 | 14 | |
| α-helix | 439-454 | 16 | |
| α-helix | 458-474 | 17 | |
| α-helix | 481-494 | 14 | |
| α-helix | 498-525 | 28 | |
| β-strand | 533-535 | 3 | 1 |
| β-strand | 538-540 | 3 | 2 |
| α-helix | 541-543 | 3 | |
| α-helix | 556-572 | 17 | |
| β-strand | 576-580 | 5 | 2 |
| α-helix | 582-584 | 3 | |
| β-strand | 586-591 | 6 | 1 |
| β-strand | 599-603 | 5 | 1 |
| α-helix | 604-610 | 7 | |
| α-helix | 611-614 | 4 | |
| β-strand | 618-620 | 3 | 3 |
| α-helix | 621-627 | 7 | |
| α-helix | 632-645 | 14 | |
| β-strand | 648-649 | 2 | 3 |
| α-helix | 657-659 | 3 | |
| β-strand | 667-670 | 4 | 3 |
| β-strand | 680-682 | 3 | 1 |
| α-helix | 688-718 | 31 | |
| β-strand | 723-725 | 3 | 4 |
| α-helix | 726-737 | 12 | |
| α-helix | 745-757 | 13 | |
| β-strand | 761-764 | 4 | 4 |
| β-strand | 767-773 | 7 | 4 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| β-strand | 22-28 | 7 | 1 |
| β-strand | 31-35 | 5 | 2 |
| α-helix | 54-58 | 5 | |
| α-helix | 60 | 1 | |
| β-strand | 70-73 | 4 | 5 |
| β-strand | 78-80 | 3 | 5 |
| α-helix | 81-87 | 7 | |
| β-strand | 93 | 1 | 6 |
| β-strand | 100 | 1 | 6 |
| β-strand | 103-105 | 3 | 5 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| α-helix | 6-14 | 9 | |
| α-helix | 20-33 | 14 | |
| α-helix | 45-56 | 12 | |
| α-helix | 62-76 | 15 | |
| α-helix | 81-94 | 14 | |
| α-helix | 101-116 | 16 | |
| α-helix | 127-142 | 16 | |
| α-helix | 148-164 | 17 | |
| α-helix | 173-180 | 8 | |
| α-helix | 181-185 | 5 | |
| α-helix | 189-202 | 14 | |
| α-helix | 210-220 | 11 | |
| α-helix | 230-240 | 11 | |
| α-helix | 243-245 | 3 | |
| α-helix | 252-260 | 9 | |
| α-helix | 268-280 | 13 | |
| α-helix | 287-297 | 11 | |
| α-helix | 348-361 | 14 | |
| α-helix | 368-372 | 5 | |
| α-helix | 376-380 | 5 | |
| α-helix | 389-405 | 17 | |
| α-helix | 424-431 | 8 | |
| α-helix | 434-442 | 9 | |
| α-helix | 448-464 | 17 | |
| α-helix | 470-472 | 3 | |
| α-helix | 473-483 | 11 | |
| α-helix | 491-506 | 16 | |
| α-helix | 510-513 | 4 | |
| α-helix | 514-517 | 4 | |
| α-helix | 521-528 | 8 | |
| α-helix | 533-550 | 18 | |
| α-helix | 562-576 | 15 | |
| α-helix | 583-599 | 17 | |
| α-helix | 601-603 | 3 | |
| α-helix | 607-618 | 12 | |
| α-helix | 624-635 | 12 | |
| α-helix | 645-658 | 14 | |
| α-helix | 664-680 | 17 | |
| α-helix | 687-694 | 8 | |
| α-helix | 698-700 | 3 | |
| α-helix | 706-719 | 14 | |
| α-helix | 724-729 | 6 | |
| α-helix | 735-742 | 8 | |
| α-helix | 749-763 | 15 | |
| α-helix | 772-779 | 8 | |
| α-helix | 793-809 | 17 | |
| α-helix | 815-818 | 4 | |
| α-helix | 832-848 | 17 | |
| α-helix | 856-863 | 8 | |
| α-helix | 864-866 | 3 | |
| α-helix | 870-886 | 17 | |
| α-helix | 888-900 | 13 | |
| α-helix | 903-905 | 3 | |
| α-helix | 906-918 | 13 | |
| α-helix | 926-936 | 11 | |
| α-helix | 947-960 | 14 | |
| α-helix | 963-965 | 3 | |
| α-helix | 967-970 | 4 | |
| α-helix | 979-988 | 10 | |
| α-helix | 990-992 | 3 | |
| α-helix | 1000-1007 | 8 | |
| α-helix | 1012-1015 | 4 | |
| α-helix | 1021-1036 | 16 | |
| α-helix | 1038-1040 | 3 | |
| α-helix | 1042-1044 | 3 | |
| α-helix | 1045-1054 | 10 | |
| α-helix | 1060-1062 | 3 | |
| β-strand | 1063-1068 | 6 | 7 |
| β-strand | 1070-1076 | 7 | 7 |
| α-helix | 1078-1094 | 17 | |
| α-helix | 1102-1111 | 10 | |
| α-helix | 1117-1132 | 16 | |
| α-helix | 1136-1139 | 4 | |
| α-helix | 1146-1154 | 9 | |
| α-helix | 1163-1182 | 20 | |
| α-helix | 1200-1208 | 9 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| Cullin homolog 1 | A | protein | 776 | Homo sapiens | Q13616 (AlphaFold model) |
| RING-box protein 1 | B | protein | 108 | Homo sapiens | P62877 (AlphaFold model) |
| TIP120 protein | C | protein | 1230 | Homo sapiens | Q86VP6 (AlphaFold model) |
>1U6G_1 Cullin homolog 1 (chains A) MSSTRSQNPHGLKQIGLDQIWDDLRAGIQQVYTRQSMAKSRYMELYTHVYNYCTSVHQSN QARGAGVPPSKSKKGQTPGGAQFVGLELYKRLKEFLKNYLTNLLKDGEDLMDESVLKFYT QQWEDYRFSSKVLNGICAYLNRHWVRRECDEGRKGIYEIYSLALVTWRDCLFRPLNKQVT NAVLKLIEKERNGETINTRLISGVVQSYVELGLNEDDAFAKGPTLTVYKESFESQFLADT ERFYTRESTEFLQQNPVTEYMKKAEARLLEEQRRVQVYLHESTQDELARKCEQVLIEKHL EIFHTEFQNLLDADKNEDLGRMYNLVSRIQDGLGELKKLLETHIHNQGLAAIEKCGEAAL NDPKMYVQTVLDVHKKYNALVMSAFNNDAGFVAALDKACGRFINNNAVTKMAQSSSKSPE LLARYCDSLLKKSSKNPEEAELEDTLNQVMVVFKYIEDKDVFQKFYAKMLAKRLVHQNSA SDDAEASMISKLKQACGFEYTSKLQRMFQDIGVSKDLNEQFKKHLTNSEPLDLDFSIQVL SSGSWPFQQSCTFALPSELERSYQRFTAFYASRHSGRKLTWLYQLSKGELVTNCFKNRYT LQASTFQMAILLQYNTEDAYTVQQLTDSTQIKMDILAQVLQILLKSKLLVLEDENANVDE VELKPDTLIKLYLGYKNKKLRVNINVPMKTEQKQEQETTHKNIEEDRKLLIQAAIVRIMK MRKVLKHQQLLGEVLTQLSSRFKPRVPVIKKCIDILIEKEYLERVDGEKDTYSYLA
>1U6G_2 RING-box protein 1 (chains B) MAAAMDVDTPSGTNSGAGKKRFEVKKWNAVALWAWDIVVDNCAICRNHIMDLCIECQANQ ASATSEECTVAWGVCNHAFHFHCISRWLKTRQVCPLDNREWEFQKYGH
>1U6G_3 TIP120 protein (chains C) MASASYHISNLLEKMTSSDKDFRFMATNDLMTELQKDSIKLDDDSERKVVKMILKLLEDK NGEVQNLAVKCLGPLVSKVKEYQVETIVDTLCTNMLSDKEQLRDISSIGLKTVIGELPPA SSGSALAANVCKKITGRLTSAIAKQEDVSVQLEALDIMADMLSRQGGLLVNFHPSILTCL LPQLTSPRLAVRKRTIIALGHLVMSCGNIVFVDLIEHLLSELSKNDSMSTTRTYIQCIAA ISRQAGHRIGEYLEKIIPLVVKFCNVDDDELREYCIQAFESFVRRCPKEVYPHVSTIINI CLKYLTYDPNYNYDDEDEDENAMDADGGDDDDQGSDDEYSDDDDMSWKVRRAAAKCLDAV VSTRHEMLPEFYKTVSPALISRFKEREENVKADVFHAYLSLLKQTRPVQSWLCDPDAMEQ GETPLTMLQSQVPNIVKALHKQMKEKSVKTRQCCFNMLTELVNVLPGALTQHIPVLVPGI IFSLNDKSSSSNLKIDALSCLYVILCNHSPQVFHPHVQALVPPVVACVGDPFYKITSEAL LVTQQLVKVIRPLDQPSSFDATPYIKDLFTCTIKRLKAADIDQEVKERAISCMGQIICNL GDNLGSDLPNTLQIFLERLKNEITRLTTVKALTLIAGSPLKIDLRPVLGEGVPILASFLR KNQRALKLGTLSALDILIKNYSDSLTAAMIDAVLDELPPLISESDMHVSQMAISFLTTLA KVYPSSLSKISGSILNELIGLVRSPLLQGGALSAMLDFFQALVVTGTNNLGYMDLLRMLT GPVYSQSTALTHKQSYYSIAKCVAALTRACPKEGPAVVGQFIQDVKNSRSTDSIRLLALL SLGEVGHHIDLSGQLELKSVILEAFSSPSEEVKSAASYALGSISVGNLPEYLPFVLQEIT SQPKRQYLLLHSLKEIISSASVVGLKPYVENIWALLLKHCECAEEGTRNVVAECLGKLTL IDPETLLPRLKGYLISGSSYARSSVVTAVKFTISDHPQPIDPLLKNCIGDFLKTLEDPDL NVRRVALVTFNSAAHNKPSLIRDLLDTVLPHLYNETKVRKELIREVEMGPFKHTVDDGLD IRKAAFECMYTLLDSCLDRLDIFEFLNHVEDGLKDHYDIKMLTFLMLVRLSTLCPSAVLQ RLDRLVEPLRATCTTKVKANSVKQEFEKQDELKRSAMRAVAALLTIPEAEKSPLMSEFQS QISSNPELAAIFESIQKDSSSTNLESMDTS
| ID | Name | Formula | Copies |
|---|---|---|---|
| ZN | Zinc ion | Zn | 3 |
Structure of the Cand1-Cul1-Roc1 complex reveals regulatory mechanisms for the assembly of the multisubunit cullin-dependent ubiquitin ligases. Goldenberg, S.J., Cascio, T.C., Shumway, S.D. et al. Cell (2004) 119:517-528. DOI 10.1016/j.cell.2004.10.019 · 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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