6Q0V: DDB1-DDA1-DCAF15 complex
Structure of DDB1-DDA1-DCAF15 complex bound to tasisulam and RBM39. Determined by X-ray diffraction at 2.9 Å resolution. Released 13 Nov 2019.
- Method
- X-ray diffraction
- Resolution
- 2.9 Å
- Organism
- Homo sapiens
- Chains
- 5
- Atoms
- 10,494
- Mol. weight
- 185.02 kDa
- Ligands
- P7M, ZN
- Released
- 13 Nov 2019
Explore 6Q0V in 3D
Show helices and sheets
RCSB PDB
PDBe
Secondary structure: helices and β-sheets
6Q0V contains 34 α-helices and 101 β-strands across 5 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: 13 helices, 66 β-strands
| Element | Residues | Length | Sheet |
|---|
| β-strand | 4-10 | 7 | 1 |
| β-strand | 17-21 | 5 | 2 |
| β-strand | 30-35 | 6 | 2 |
| β-strand | 38-43 | 6 | 2 |
| β-strand | 50-56 | 7 | 2 |
| β-strand | 61-67 | 7 | 3 |
| β-strand | 76-81 | 6 | 3 |
| β-strand | 85-94 | 10 | 3 |
| β-strand | 97-107 | 11 | 3 |
| β-strand | 115 | 1 | 4 |
| β-strand | 121-124 | 4 | 4 |
| β-strand | 130-136 | 7 | 4 |
| β-strand | 139-144 | 6 | 4 |
| β-strand | 151-154 | 4 | 3 |
| β-strand | 155-158 | 4 | 4 |
| β-strand | 164-169 | 6 | 5 |
| α-helix | 170 | 1 | |
| β-strand | 177-184 | 8 | 5 |
| β-strand | 187-196 | 10 | 5 |
| β-strand | 201-204 | 4 | 5 |
| β-strand | 210-212 | 3 | 5 |
| β-strand | 218-221 | 4 | 6 |
| β-strand | 229-232 | 4 | 6 |
| β-strand | 237-241 | 5 | 6 |
| β-strand | 244-248 | 5 | 6 |
| α-helix | 251-253 | 3 | |
| β-strand | 258-263 | 6 | 7 |
| β-strand | 270-275 | 6 | 7 |
| β-strand | 279-289 | 11 | 7 |
| β-strand | 295-307 | 13 | 7 |
| β-strand | 311-316 | 6 | 8 |
| β-strand | 321-326 | 6 | 8 |
| β-strand | 331-336 | 6 | 8 |
| β-strand | 347-353 | 7 | 8 |
| β-strand | 361-363 | 3 | 9 |
| β-strand | 375-379 | 5 | 9 |
| α-helix | 382-384 | 3 | |
| β-strand | 386-391 | 6 | 9 |
| β-strand | 711-716 | 6 | 9 |
| β-strand | 720-727 | 8 | 10 |
| α-helix | 728-730 | 3 | |
| β-strand | 732-743 | 12 | 10 |
| β-strand | 749-751 | 3 | 10 |
| α-helix | 756-758 | 3 | |
| β-strand | 762-765 | 4 | 10 |
| β-strand | 786-795 | 10 | 10 |
| β-strand | 801-806 | 6 | 10 |
| α-helix | 807-808 | 2 | |
| β-strand | 811-820 | 10 | 11 |
| β-strand | 827-835 | 9 | 11 |
| β-strand | 846-854 | 9 | 11 |
| β-strand | 857-866 | 10 | 11 |
| β-strand | 870-876 | 7 | 12 |
| β-strand | 879-884 | 6 | 12 |
| β-strand | 887-893 | 7 | 12 |
| β-strand | 899-905 | 7 | 12 |
| β-strand | 911-917 | 7 | 13 |
| β-strand | 920-925 | 6 | 13 |
| β-strand | 930-936 | 7 | 13 |
| β-strand | 941-947 | 7 | 13 |
| β-strand | 954-961 | 8 | 14 |
| β-strand | 964-969 | 6 | 14 |
| β-strand | 973-979 | 7 | 14 |
| α-helix | 986-989 | 4 | |
| β-strand | 991 | 1 | 13 |
| β-strand | 992-999 | 8 | 14 |
| β-strand | 1004-1009 | 6 | 1 |
| β-strand | 1025-1032 | 8 | 1 |
| β-strand | 1037-1042 | 6 | 1 |
| α-helix | 1045-1061 | 17 | |
| α-helix | 1070-1074 | 5 | |
| β-strand | 1076-1077 | 2 | 15 |
| β-strand | 1082-1083 | 2 | 15 |
| β-strand | 1086 | 1 | 14 |
| β-strand | 1088-1090 | 3 | 1 |
| α-helix | 1091-1095 | 5 | |
| α-helix | 1096-1099 | 4 | |
| α-helix | 1102-1108 | 7 | |
| α-helix | 1126-1137 | 12 | |
Chain B: 12 helices, 15 β-strands
| Element | Residues | Length | Sheet |
|---|
| α-helix | 36-46 | 11 | |
| α-helix | 51-53 | 3 | |
| α-helix | 58-59 | 2 | |
| β-strand | 61-64 | 4 | 16 |
| α-helix | 65-68 | 4 | |
| α-helix | 71-76 | 6 | |
| β-strand | 79-83 | 5 | 17 |
| β-strand | 89-96 | 8 | 17 |
| β-strand | 105 | 1 | 18 |
| β-strand | 106-113 | 8 | 17 |
| α-helix | 119-120 | 2 | |
| β-strand | 121-128 | 8 | 17 |
| β-strand | 134 | 1 | 18 |
| β-strand | 139-144 | 6 | 19 |
| β-strand | 151-157 | 7 | 19 |
| β-strand | 162 | 1 | 20 |
| α-helix | 172 | 1 | |
| β-strand | 173 | 1 | 20 |
| α-helix | 174 | 1 | |
| β-strand | 178-186 | 9 | 19 |
| α-helix | 187-189 | 3 | |
| α-helix | 194-197 | 4 | |
| β-strand | 217-224 | 8 | 19 |
| α-helix | 228-231 | 4 | |
| α-helix | 233-236 | 4 | |
| β-strand | 242-246 | 5 | 21 |
| β-strand | 250-258 | 9 | 21 |
Chain C: 4 helices, 12 β-strands
| Element | Residues | Length | Sheet |
|---|
| β-strand | 387-394 | 8 | 21 |
| β-strand | 420 | 1 | 19 |
| β-strand | 430 | 1 | 21 |
| β-strand | 441-449 | 9 | 21 |
| α-helix | 450-461 | 12 | |
| α-helix | 463-466 | 4 | |
| β-strand | 468-482 | 15 | 22 |
| β-strand | 487-498 | 12 | 22 |
| β-strand | 511-522 | 12 | 22 |
| β-strand | 528-533 | 6 | 22 |
| β-strand | 537-538 | 2 | 22 |
| α-helix | 544-562 | 19 | |
| β-strand | 573-575 | 3 | 19 |
| β-strand | 588-591 | 4 | 16 |
| α-helix | 592-594 | 3 | |
| β-strand | 596-599 | 4 | 16 |
Chain D: 3 helices, 6 β-strands
| Element | Residues | Length | Sheet |
|---|
| β-strand | 250-255 | 6 | 23 |
| α-helix | 263-270 | 8 | |
| α-helix | 271-273 | 3 | |
| β-strand | 276-283 | 8 | 23 |
| β-strand | 290-298 | 9 | 23 |
| α-helix | 301-311 | 11 | |
| β-strand | 315-316 | 2 | 24 |
| β-strand | 319-320 | 2 | 24 |
| β-strand | 322-324 | 3 | 23 |
Chain E: 2 helices, 2 β-strands
| Element | Residues | Length | Sheet |
|---|
| α-helix | 14-17 | 4 | |
| β-strand | 34 | 1 | 2 |
| β-strand | 46-49 | 4 | 3 |
| α-helix | 54-71 | 18 | |
Molecules and chains
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|
| DNA damage-binding protein 1 | A | protein | 864 | Homo sapiens | Q16531 (AlphaFold model) |
| DDB1- and CUL4-associated factor 15 | B | protein | 276 | Homo sapiens | Q66K64 (AlphaFold model) |
| DDB1- and CUL4-associated factor 15 | C | protein | 263 | Homo sapiens | Q66K64 (AlphaFold model) |
| RNA-binding protein 39 | D | protein | 107 | Homo sapiens | Q14498 (AlphaFold model) |
| DET1- and DDB1-associated protein 1 | E | protein | 126 | Homo sapiens | Q9BW61 (AlphaFold model) |
Sequence of entity 1 (A), FASTA
>6Q0V_1 DNA damage-binding protein 1 (chains A)
MGSSHHHHHHSAAHIVMVDAYKPTKGGRMSYNYVVTAQKPTAVNGCVTGHFTSAEDLNLL
IAKNTRLEIYVVTAEGLRPVKEVGMYGKIAVMELFRPKGESKDLLFILTAKYNACILEYK
QSGESIDIITRAHGNVQDRIGRPSETGIIGIIDPECRMIGLRLYDGLFKVIPLDRDNKEL
KAFNIRLEELHVIDVKFLYGCQAPTICFVYQDPQGRHVKTYEVSLREKEFNKGPWKQENV
EAEASMVIAVPEPFGGAIIIGQESITYHNGDKYLAIAPPIIKQSTIVCHNRVDPNGSRYL
LGDMEGRLFMLLLEKEEQMDGTVTLKDLRVELLGETSIAECLTYLDNGVVFVGSRLGDSQ
LVKLNVDSNEQGSYVVAMETFTNLGPIVDMCVVDLERQGQGQLVTCSGAFKEGSLRIIRN
GIGGNGNSGEIQKLHIRTVPLYESPRKICYQEVSQCFGVLSSRIEVQDTSGGTTALRPSA
STQALSSSVSSSKLFSSSTAPHETSFGEEVEVHNLLIIDQHTFEVLHAHQFLQNEYALSL
VSCKLGKDPNTYFIVGTAMVYPEEAEPKQGRIVVFQYSDGKLQTVAEKEVKGAVYSMVEF
NGKLLASINSTVRLYEWTTEKELRTECNHYNNIMALYLKTKGDFILVGDLMRSVLLLAYK
PMEGNFEEIARDFNPNWMSAVEILDDDNFLGAENAFNLFVCQKDSAATTDEERQHLQEVG
LFHLGEFVNVFCHGSLVMQNLGETSTPTQGSVLFGTVNGMIGLVTSLSESWYNLLLDMQN
RLNKVIKSVGKIEHSFWRSFHTERKTEPATGFIDGDLIESFLDISRPKMQEVVANLQYDD
GSGMKREATADDLIKVVEELTRIH
Sequence of entity 2 (B), FASTA
>6Q0V_2 DDB1- and CUL4-associated factor 15 (chains B)
MDWSHPQFEKSAVGLNDIFEAQKIEWHEGGGGSGENLYFQGGGRMGRRREHVLKQLERVK
ISGQLSPRLFRKLPPRVCVSLKNIVDEDFLYAGHIFLGFSKCGRYVLSYTSSSGDDDFSF
YIYHLYWWEFNVHSKLKLVRQVRLFQDEEIYSDLYLTVCEWPSDASKVIVFGFNTRSANG
MLMNMMMMSDENHRDIYVSTVAVPPPGRCAACQDASRAHPGDPNAQCLRHGFMLHTKYQV
VYPFPTFQPAFQLKKDQVVLLNTSYSLVACAVSVHS
Sequence of entity 3 (C), FASTA
>6Q0V_3 DDB1- and CUL4-associated factor 15 (chains C)
MDWSHPQFEKSAVGLNDIFEAQKIEWHEGGGGSGENLYFQGGGRMEPGYVNYTKLYYVLE
SGEGTEPEDELEDDKISLPFVVTDLRGRNLRPMRERTAVQGQYLTVEQLTLDFEYVINEV
IRHDATWGHQFCSFSDYDIVILEVCPETNQVLINIGLLLLAFPSPTEEGQLRPKTYHTSL
KVAWDLNTGIFETVSVGDLTEVKGQTSGSVWSSYRKSCVDMVMKWLVPESSGRYVNRMTN
EALHKGCSLKVLADSERYTWIVL
Sequence of entity 4 (D), FASTA
>6Q0V_4 RNA-binding protein 39 (chains D)
MGSSHHHHHHSAVDENLYFQGGGRMRLYVGSLHFNITEDMLRGIFEPFGRIESIQLMMDS
ETGRSKGYGFITFSDSECAKKALEQLNGFELAGRPMKVGHVTERTDA
Sequence of entity 5 (E), FASTA
>6Q0V_5 DET1- and DDB1-associated protein 1 (chains E)
MGSSHHHHHHSAVDENLYFQGGGRMADFLKGLPVYNKSNFSRFHADSVCKASNRRPSVYL
PTREYPSEQIIVTEKTNILLRYLHQQWDKKNAAKKRDQEQVELEGESSAPPRKVARTDSP
DMHEDT
Ligands and cofactors
| ID | Name | Formula | Copies |
|---|
| P7M | N-[(5-bromothiophen-2-yl)sulfonyl]-2,4-dichlorobenzamide | C11 H6 Br Cl2 N O3 S2 | 1 |
| ZN | Zinc ion | Zn | 1 |
Primary citation
Structural complementarity facilitates E7820-mediated degradation of RBM39 by DCAF15. Faust, T.B., Yoon, H., Nowak, R.P. et al. Nat Chem Biol (2020) 16:7-14. DOI 10.1038/s41589-019-0378-3 · PubMed
Other PDB entries of the same protein (UniProt Q16531 (AlphaFold model), which also has an AlphaFold model), best resolution first:
- 9BBG 1.7 Å, Co-crystal structure of human DDB1 bound to fragment UB028671
- 9EJQ 1.87 Å, Crystal structure of DDB1 in complex with XS381952
- 9BBI 1.9 Å, Co-crystal structure of human DDB1 bound to fragment UB028669
- 9BZ0 1.9 Å, Structure of an STK19-containing TC-NER complex
- 9BBE 2.0 Å, Co-crystal structure of human DDB1 bound to fragment UB028668
- 9BBH 2.0 Å, Co-crystal structure of human DDB1 bound to fragment UB028670
- 9FJX 2.0 Å, Crystal structure of human CRBN-DDB1 in complex with Lenalidomide
- 9ZXN 2.07 Å, DDB1 delta with compound 26
- 37MF 2.1 Å, Crystal structure of DDB1 in complex with XS445479
- 9ZXM 2.19 Å, DDB1 delta with compound 6
- 8G46 2.2 Å, Cryo-EM structure of DDB1deltaB-DDA1-DCAF16-BRD4(BD2)-MMH2
- 8ZSW 2.25 Å, Crystal Structure of Human DDB1, a Component of the E3 Ubiquitin Ligase Complex
Browse structure collections
About this viewer
MolViewer shows 6Q0V directly in your browser with nothing to install. Switch between cartoon, ball-and-stick, spacefill and surface views, color by chain, secondary structure or B-factor, measure distances, angles and dihedrals, and share or embed the view.