6ZZ6: S.cerevisiae cohesin-Scc2-DNA complex

Cryo-EM structure of S.cerevisiae cohesin-Scc2-DNA complex. Determined by electron microscopy at 3.4 Å resolution. Released 30 Sept 2020.

Method
Electron microscopy
Resolution
3.4 Å
Organisms
Saccharomyces cerevisiae (strain ATCC 204508 / S288c), synthetic construct
Chains
6
Atoms
16,597
Mol. weight
291.55 kDa
Ligands
ATP, MG
Released
30 Sept 2020

Explore 6ZZ6 in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

6ZZ6 contains 85 α-helices and 35 β-strands across 4 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: 10 helices, 15 β-strands

ElementResiduesLengthSheet
β-strand3-1081
β-strand18-2251
β-strand28-3252
α-helix39-4911
α-helix55-573
β-strand7013
β-strand92-10091
β-strand103-11191
β-strand117-12151
β-strand124-12631
α-helix128-13710
β-strand148-14922
α-helix156-1594
α-helix162-17312
α-helix179-19416
α-helix1045-108339
β-strand1096-110164
β-strand1112-111764
α-helix1131-114818
β-strand1153-115642
α-helix1165-117814
β-strand1184-118852
α-helix1195-11973
β-strand1200-120782
β-strand1212-121762
Chain B: 10 helices, 14 β-strands
ElementResiduesLengthSheet
β-strand5-955
β-strand17-2045
β-strand27-3156
α-helix38-4811
α-helix58-647
β-strand76-8165
β-strand104-10965
β-strand114-11745
α-helix126-13510
β-strand145-14626
α-helix151-1566
α-helix159-16911
α-helix172-22756
α-helix999-105961
β-strand1067-107047
β-strand1106-110947
β-strand111913
α-helix1128-114518
β-strand1150-115456
α-helix1162-117514
β-strand1180-118456
β-strand1196-120276
β-strand1207-121266
α-helix1214-12218
Chain C: 4 helices, 3 β-strands
ElementResiduesLengthSheet
α-helix70-10233
β-strand50318
α-helix504-5096
α-helix521-53717
β-strand541-54448
α-helix549-5502
β-strand551-55448
Chain D: 61 helices, 3 β-strands
ElementResiduesLengthSheet
α-helix222-23514
α-helix251-26111
α-helix279-29012
α-helix305-32117
α-helix339-35113
α-helix357-37216
α-helix387-40519
α-helix410-41910
α-helix421-4233
β-strand434-43529
β-strand442-44329
α-helix445-45511
α-helix460-4656
α-helix476-50530
α-helix511-52313
α-helix532-54716
α-helix556-57823
α-helix598-61518
α-helix619-63315
α-helix648-66114
α-helix679-6879
α-helix692-6954
α-helix697-70812
α-helix713-72917
α-helix737-74812
α-helix752-76413
α-helix769-7713
α-helix772-7776
α-helix784-80017
α-helix804-81613
α-helix823-83412
α-helix835-8395
α-helix840-8445
α-helix851-86515
α-helix871-88212
α-helix893-91624
α-helix928-94114
α-helix950-96112
α-helix968-98013
α-helix988-100013
α-helix1007-102115
α-helix1028-104821
α-helix1061-107414
α-helix1093-110311
α-helix1111-112717
α-helix1129-11335
α-helix1135-114612
α-helix1152-117423
β-strand1179-118135
α-helix1204-12118
α-helix1213-12208
α-helix1225-124117
α-helix1246-12483
α-helix1250-12578
α-helix1262-128524
α-helix1287-130115
α-helix1313-13197
α-helix1326-134015
α-helix1356-136712
α-helix1369-13713
α-helix1374-139724
α-helix1414-143320
α-helix1449-14535
α-helix1467-14726

Molecules and chains

MoleculeChainsTypeLengthOrganismUniProt
Structural maintenance of chromosomes protein 1,Structural maintenance of chromosomes protein…Aprotein360Saccharomyces cerevisiae (strain ATCC 204508 / S288c)P32908 (AlphaFold model)
Structural maintenance of chromosomes protein 3,Structural maintenance of chromosomes protein…Bprotein423Saccharomyces cerevisiae (strain ATCC 204508 / S288c)P47037 (AlphaFold model)
Sister chromatid cohesion protein 1,Sister chromatid cohesion protein 1,Sister chromatid cohesion…Cprotein83Saccharomyces cerevisiae (strain ATCC 204508 / S288c)Q12158 (AlphaFold model)
Sister chromatid cohesion protein 2Dprotein1493Saccharomyces cerevisiae (strain ATCC 204508 / S288c)Q04002 (AlphaFold model)
DNA (34-mer)FDNA34synthetic construct
DNA (34-mer)GDNA34synthetic construct
Sequence of entity 1 (A), FASTA
>6ZZ6_1 Structural maintenance of chromosomes protein 1,Structural maintenance of chromosomes protein 1,Structural maintenance of chromosomes protein 1 (chains A)
GRLVGLELSNFKSYRGVTKVGFGESNFTSIIGPNGSGKSNMMDAISFVLGVRSNHLRSNI
LKDLIYRGVLSNPQSAYVKAFYQKGNKLVELMRIISRNGDTSYKIDGKTVSYKDYSIFLE
NENILIKAKNFLVFQGDVEQIAAQSPVELSRMFEEVSGSIQYKKEYEELKEKIEKLSKSA
EEKKILNQFLKIKKKRKELFEKTFDYVSDHLDAIYRELTKNPNSNVELAGGNASLTIEDE
DEPFNAGIKYHATPPLKRFKDMEYLSGGEKTVAALALLFAINSYQPSPFFVLDQVDAALD
ITNVQRIAAYIRRHRNPDLQFIVISLKNTMFEKSDALVGVYRQQQENSSKIITLDLSNYA
Sequence of entity 2 (B), FASTA
>6ZZ6_2 Structural maintenance of chromosomes protein 3,Structural maintenance of chromosomes protein 3,Structural maintenance of chromosomes protein 3 (chains B)
GPYIKRVIIKGFKTYRNETIIDNFSPHQNVIIGSNGSGKSNFFAAIRFVLSDDYSNLKRE
ERQGLIHQGSGGSVMSASVEIVFHDPDHSMILPSGVLSRGDDEVTIRRTVGLKKDDYQLN
DRNVTKGDIVRMLETAGFSMNNPYNIVPQGKIVALTNAKDKERLQLLEDVVGAKSFEVKL
KASLKKMEETEQKKIQINKEMGELNSKLSEMEQERKELEKYNELERNRKRAFENFKKFNE
RRKDLAERASELDESKDSIQDLIVKLKQQKVNAVDSTFQKVSENFEAVFERLVPRGTAKL
IIHRYTGVSISVSFNSKQNEQLHVEQLSGGQKTVCAIALILAIQMVDPASFYLFDQIDAA
LDKQYRTAVATLLKELSKNAQFICTTFRTDMLQVADKFFRVKYENKISTVIEVNREEAIG
FIR
Sequence of entity 3 (C), FASTA
>6ZZ6_3 Sister chromatid cohesion protein 1,Sister chromatid cohesion protein 1,Sister chromatid cohesion protein 1 (chains C)
TLRTSGELLQGIVRVYSKQATFLLTDIKDTLTKISMLVIFTDVLKSITKREASRGFFDIL
SLATEGCIGLSQTEAFGNIKIDA
Sequence of entity 4 (D), FASTA
>6ZZ6_4 Sister chromatid cohesion protein 2 (chains D)
MSYPGKDKNIPGRIIEALEDLPLSYLVPKDGLAALVNAPMRVSLPFDKTIFTSADDGRDV
NINVLGTANSTTSSIKNEAEKERLVFKRPSNFTSSANSVDYVPTNFLEGLSPLAQSVLST
HKGLNDSINIEKKSEIVSRPEAKHKLESVTSNAGNLSFNDNSSNKKTKTSTGVTMTQANL
AEQYLNDLKNILDIVGFDQNSAEIGNIEYWLQLPNKKFVLTTNCLTKLQMTIKNITDNPQ
LSNSIEITWLLRLLDVMVCNIKFSKSSLKMGLDDSMLRYIALLSTIVLFNIFLLGKNDSN
LHRESYIMEPVNFLSDLIESLKILTIEYGSLKIEFDTFQEALELLPKYIRNGPFLDDNVT
AKLVYIFSDLLMNNDIEATTNIQFQSFWDNVKRISSDILVSLFGSFDQQRGFIIEELLSH
IEKLPTKRIQKKLRKVGNQNIYITDFTFTLMSMLENINCYSFCNQMKDIAPENIDLLKNE
YKKQEEFLFNIVEHINDTILERFFKNPSALRYVIDNFVQDLLLLISSPQWPVTEKILSSL
LKRLLSVYSPSMQVSANIETICLQLIGNIGSTIFDIKCSTRDHEDNNLIKMINYPETLPH
FFKSFEECIAYNETIKCRRSATRFLWNLRLGTILILEEYTKDAKEQIITVDNELKKILEQ
IKDGGLGPELENREADFSTIKLDYFSILHAFELLNLYDPYLKLILSLLAKDKIKLRSTAI
KCLSMLASKDKVILSNPMVKETIHRRLNDSSASVKDAILDLVSINSSYFEFYQQINNNYN
DDSIMVRKHVLRINEKMYDETNDIVTKVYVIARILMKIEDEEDNIIDMARLILLNRWILK
VHEVLDQPEKLKEISSSVLLVMSRVAIMNEKCSQLFDLFLNFYLLNKEAHSKEAYDKITH
VLTILTDFLVQKIVELNSDDTNEKNSIVDKQNFLNLLAKFADSTVSFLTKDHITALYPYM
VSDEKSDFHYYILQVFRCTFEKLANFKQKFLYDLETTLLSRLPKMNVREIDEAMPLIWSV
ATHRHDTARVAKACSSCLSHLHPYINKANNEEAAIVVDGKLQRLIYLSTGFARFCFPKPS
NDKIAFLQEGETLYEHITKCLLVLSKDKITHVIRRVAVKNLTKLCGNHPKLFNSRHVLHL
LDKEFQSDQLDIKLVILESLYDLFLLEERKSVRNTGVNSTLSSNSILKKKLLKTNRVEFA
NDGVCSALATRFLDNILQLCLLRDLKNSLVAIRLLKLILKFGYTNPSHSIPTVIALFAST
SQYIRHVAYELLEDLFEKYETLVFSSLSRGVTKAIHYSIHTDEKYYYKHDHFLSLLEKLC
GTGKKNGPKFFKVLKRIMQSYLDDITDLTSTNSSVQKSIFVLCTNISNITFVSQYDLVSL
LKTIDLTTDRLKEVIMDEIGDNVSSLSVSEEKLSGIILIQLSLQDLGTYLLHLYGLRDDV
LLLDIVEESELKNKQLPAKKPDISKFSAQLENIEQYSSNGKLLTYFRKHVKDT
Sequence of entity 5 (F), FASTA
>6ZZ6_5 DNA (34-MER) (chains F)
AAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAA
Sequence of entity 6 (G), FASTA
>6ZZ6_6 DNA (34-MER) (chains G)
TTTTTTTTTTTTTTTTTTTTTTTTTTTTTTTTTT

Ligands and cofactors

IDNameFormulaCopies
ATPAdenosine-5'-triphosphateC10 H16 N5 O13 P32
MGMagnesium ionMg2

Primary citation

Transport of DNA within cohesin involves clamping on top of engaged heads by Scc2 and entrapment within the ring by Scc3. Collier, J.E., Lee, B.G., Roig, M.B. et al. Elife (2020) 9. DOI 10.7554/eLife.59560 · PubMed

Other PDB entries of the same protein (UniProt P32908 (AlphaFold model), which also has an AlphaFold model), best resolution first:

Browse structure collections

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