6Q0W: DDB1-DDA1-DCAF15 complex

Structure of DDB1-DDA1-DCAF15 complex bound to Indisulam 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
10,558
Mol. weight
184.99 kDa
Ligands
ZN, EF6
Released
13 Nov 2019

Explore 6Q0W in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

6Q0W contains 37 α-helices and 102 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: 15 helices, 67 β-strands

ElementResiduesLengthSheet
β-strand4-1071
β-strand17-2152
β-strand30-3562
β-strand38-4362
β-strand50-5672
β-strand61-6773
β-strand76-8163
β-strand85-94103
β-strand97-107113
β-strand11514
β-strand121-12445
β-strand130-13455
β-strand13614
β-strand139-14465
β-strand151-15443
β-strand155-15845
β-strand164-16966
α-helix1701
β-strand177-18486
β-strand187-196106
β-strand201-20446
β-strand210-21236
β-strand218-22147
α-helix222-2232
β-strand229-23247
β-strand237-24157
β-strand244-24857
α-helix251-2533
β-strand258-26368
β-strand270-27568
β-strand279-289118
β-strand295-307138
β-strand313-31649
β-strand321-32559
β-strand331-33669
β-strand347-35379
β-strand359-365710
β-strand374-379610
α-helix382-3843
β-strand386-391610
β-strand711-716610
β-strand720-727811
α-helix728-7303
β-strand732-7431211
β-strand749-751311
α-helix756-7583
β-strand762-765411
β-strand786-7951011
β-strand801-806611
α-helix807-8082
β-strand811-819912
β-strand828-835812
β-strand846-854912
β-strand857-8661012
β-strand870-876713
β-strand879-884613
β-strand887-893713
β-strand899-905713
β-strand911-917714
β-strand920-925614
β-strand930-936714
β-strand941-947714
β-strand954-961815
β-strand964-969615
β-strand973-979715
α-helix986-9894
β-strand991114
β-strand992-999815
β-strand1004-100961
β-strand1025-103281
β-strand1037-104261
α-helix1045-106117
α-helix1065-10673
α-helix1070-10745
β-strand1076-1077216
β-strand1082-1083216
β-strand1086115
β-strand1088-109031
α-helix1091-10955
α-helix1096-10994
α-helix1102-11087
α-helix1126-113712
Chain B: 12 helices, 15 β-strands
ElementResiduesLengthSheet
α-helix36-4611
α-helix51-533
α-helix58-592
β-strand61-64417
α-helix65-684
α-helix71-733
β-strand79-83518
β-strand89-96818
β-strand105119
β-strand106-113818
α-helix119-1202
β-strand121-128818
β-strand134119
β-strand139-144620
β-strand151-157720
β-strand162121
α-helix1721
β-strand173121
α-helix1741
β-strand178-186920
α-helix187-1893
α-helix194-1974
β-strand217-224820
α-helix228-2314
α-helix233-2364
β-strand242-246522
β-strand250-258922
Chain C: 4 helices, 12 β-strands
ElementResiduesLengthSheet
β-strand387-394822
β-strand420120
β-strand430122
β-strand441-449922
α-helix450-46112
α-helix463-4664
β-strand468-4821523
β-strand487-4981223
β-strand511-5221223
β-strand528-533623
β-strand537-538223
α-helix544-56219
α-helix565-5673
β-strand573-575320
β-strand588-591417
β-strand596-599417
Chain D: 4 helices, 6 β-strands
ElementResiduesLengthSheet
β-strand250-255624
α-helix263-2708
α-helix271-2733
β-strand276-284924
β-strand289-2981024
α-helix301-31111
β-strand315125
β-strand320125
α-helix3211
β-strand322-325424
Chain E: 2 helices, 2 β-strands
ElementResiduesLengthSheet
α-helix14-163
β-strand3412
β-strand46-4943
α-helix54-7118

Molecules and chains

MoleculeChainsTypeLengthOrganismUniProt
DNA damage-binding protein 1Aprotein864Homo sapiensQ16531 (AlphaFold model)
DDB1- and CUL4-associated factor 15Bprotein276Homo sapiensQ66K64 (AlphaFold model)
DDB1- and CUL4-associated factor 15Cprotein263Homo sapiensQ66K64 (AlphaFold model)
RNA-binding protein 39Dprotein107Homo sapiensQ14498 (AlphaFold model)
DET1- and DDB1-associated protein 1Eprotein126Homo sapiensQ9BW61 (AlphaFold model)
Sequence of entity 1 (A), FASTA
>6Q0W_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
>6Q0W_2 DDB1- and CUL4-associated factor 15 (chains B)
MDWSHPQFEKSAVGLNDIFEAQKIEWHEGGGGSGENLYFQGGGRMGRRREHVLKQLERVK
ISGQLSPRLFRKLPPRVCVSLKNIVDEDFLYAGHIFLGFSKCGRYVLSYTSSSGDDDFSF
YIYHLYWWEFNVHSKLKLVRQVRLFQDEEIYSDLYLTVCEWPSDASKVIVFGFNTRSANG
MLMNMMMMSDENHRDIYVSTVAVPPPGRCAACQDASRAHPGDPNAQCLRHGFMLHTKYQV
VYPFPTFQPAFQLKKDQVVLLNTSYSLVACAVSVHS
Sequence of entity 3 (C), FASTA
>6Q0W_3 DDB1- and CUL4-associated factor 15 (chains C)
MDWSHPQFEKSAVGLNDIFEAQKIEWHEGGGGSGENLYFQGGGRMEPGYVNYTKLYYVLE
SGEGTEPEDELEDDKISLPFVVTDLRGRNLRPMRERTAVQGQYLTVEQLTLDFEYVINEV
IRHDATWGHQFCSFSDYDIVILEVCPETNQVLINIGLLLLAFPSPTEEGQLRPKTYHTSL
KVAWDLNTGIFETVSVGDLTEVKGQTSGSVWSSYRKSCVDMVMKWLVPESSGRYVNRMTN
EALHKGCSLKVLADSERYTWIVL
Sequence of entity 4 (D), FASTA
>6Q0W_4 RNA-binding protein 39 (chains D)
MGSSHHHHHHSAVDENLYFQGGGRMRLYVGSLHFNITEDMLRGIFEPFGRIESIQLMMDS
ETGRSKGYGFITFSDSECAKKALEQLNGFELAGRPMKVGHVTERTDA
Sequence of entity 5 (E), FASTA
>6Q0W_5 DET1- and DDB1-associated protein 1 (chains E)
MGSSHHHHHHSAVDENLYFQGGGRMADFLKGLPVYNKSNFSRFHADSVCKASNRRPSVYL
PTREYPSEQIIVTEKTNILLRYLHQQWDKKNAAKKRDQEQVELEGESSAPPRKVARTDSP
DMHEDT

Ligands and cofactors

IDNameFormulaCopies
ZNZinc ionZn1
EF6N~1~-(3-chloro-1H-indol-7-yl)benzene-1,4-disulfonamideC14 H12 Cl N3 O4 S21

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:

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