6SKO: Fork Protection Complex
Cryo-EM Structure of the Fork Protection Complex Bound to CMG at a Replication Fork - conformation 2 MCM CTD:ssDNA. Determined by electron microscopy at 3.4 Å resolution. Released 6 May 2020.
- Method
- Electron microscopy
- Resolution
- 3.4 Å
- Organisms
- Saccharomyces cerevisiae (strain ATCC 204508 / S288c), synthetic construct
- Chains
- 7
- Atoms
- 15,715
- Mol. weight
- 635.42 kDa
- Ligands
- ANP, MG
- Released
- 6 May 2020
Explore 6SKO in 3D
Show helices and sheets
RCSB PDB
PDBe
Secondary structure: helices and β-sheets
6SKO contains 99 α-helices and 89 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 2: 16 helices, 14 β-strands
| Element | Residues | Length | Sheet |
|---|
| α-helix | 478-487 | 10 | |
| α-helix | 493-500 | 8 | |
| α-helix | 509-520 | 12 | |
| β-strand | 525 | 1 | 16 |
| β-strand | 533 | 1 | 16 |
| β-strand | 539-543 | 5 | 17 |
| α-helix | 549-557 | 9 | |
| β-strand | 563-566 | 4 | 17 |
| β-strand | 571 | 1 | 7 |
| α-helix | 573-577 | 5 | |
| β-strand | 578-582 | 5 | 18 |
| β-strand | 589-593 | 5 | 18 |
| β-strand | 603-607 | 5 | 17 |
| α-helix | 615-623 | 9 | |
| β-strand | 628-631 | 4 | 19 |
| α-helix | 633-635 | 3 | |
| β-strand | 638-641 | 4 | 19 |
| β-strand | 645-650 | 6 | 17 |
| α-helix | 663-666 | 4 | |
| α-helix | 671-676 | 6 | |
| β-strand | 679-683 | 5 | 17 |
| α-helix | 689-705 | 17 | |
| α-helix | 747-751 | 5 | |
| α-helix | 760-773 | 14 | |
| β-strand | 777-778 | 2 | 20 |
| α-helix | 780-799 | 20 | |
| α-helix | 807-823 | 17 | |
| β-strand | 828-829 | 2 | 20 |
| α-helix | 831-846 | 16 | |
| α-helix | 850-865 | 16 | |
Chain 3: 18 helices, 14 β-strands
| Element | Residues | Length | Sheet |
|---|
| α-helix | 344-354 | 11 | |
| α-helix | 359-366 | 8 | |
| α-helix | 375-386 | 12 | |
| β-strand | 391-392 | 2 | 26 |
| β-strand | 398-399 | 2 | 26 |
| β-strand | 405-409 | 5 | 27 |
| α-helix | 415-422 | 8 | |
| β-strand | 429-433 | 5 | 27 |
| β-strand | 437 | 1 | 24 |
| α-helix | 439-442 | 4 | |
| β-strand | 444-447 | 4 | 28 |
| β-strand | 456-459 | 4 | 28 |
| β-strand | 469-473 | 5 | 27 |
| α-helix | 475-477 | 3 | |
| α-helix | 480-492 | 13 | |
| β-strand | 494-499 | 6 | 12 |
| β-strand | 502-507 | 6 | 12 |
| β-strand | 511-516 | 6 | 27 |
| α-helix | 529-532 | 4 | |
| α-helix | 537-540 | 4 | |
| β-strand | 545-549 | 5 | 27 |
| α-helix | 555-568 | 14 | |
| α-helix | 580-582 | 3 | |
| α-helix | 653-666 | 14 | |
| α-helix | 669 | 1 | |
| β-strand | 670-671 | 2 | 29 |
| α-helix | 672 | 1 | |
| α-helix | 673-688 | 16 | |
| α-helix | 692-693 | 2 | |
| α-helix | 699-715 | 17 | |
| β-strand | 720-721 | 2 | 29 |
| α-helix | 723-737 | 15 | |
Chain 4: 19 helices, 16 β-strands
| Element | Residues | Length | Sheet |
|---|
| α-helix | 503-513 | 11 | |
| α-helix | 518-526 | 9 | |
| α-helix | 534-545 | 12 | |
| β-strand | 550-551 | 2 | 30 |
| β-strand | 557-558 | 2 | 30 |
| β-strand | 564-568 | 5 | 31 |
| α-helix | 574-584 | 11 | |
| β-strand | 588-592 | 5 | 31 |
| β-strand | 596 | 1 | 14 |
| α-helix | 598-601 | 4 | |
| β-strand | 603-606 | 4 | 32 |
| β-strand | 615-618 | 4 | 32 |
| α-helix | 622-624 | 3 | |
| β-strand | 628-632 | 5 | 31 |
| α-helix | 634-636 | 3 | |
| α-helix | 639-642 | 4 | |
| α-helix | 645-650 | 6 | |
| β-strand | 653-657 | 5 | 4 |
| β-strand | 662-666 | 5 | 4 |
| β-strand | 670-675 | 6 | 31 |
| α-helix | 688-692 | 5 | |
| α-helix | 696-699 | 4 | |
| β-strand | 704-708 | 5 | 31 |
| α-helix | 714-724 | 11 | |
| α-helix | 725-729 | 5 | |
| α-helix | 744-757 | 14 | |
| α-helix | 760 | 1 | |
| β-strand | 761-762 | 2 | 33 |
| α-helix | 763 | 1 | |
| α-helix | 764-778 | 15 | |
| α-helix | 795-811 | 17 | |
| β-strand | 816-817 | 2 | 33 |
| α-helix | 819-832 | 14 | |
| β-strand | 838 | 1 | 34 |
| β-strand | 845 | 1 | 34 |
Chain 5: 12 helices, 13 β-strands
| Element | Residues | Length | Sheet |
|---|
| α-helix | 351-362 | 12 | |
| α-helix | 366-371 | 6 | |
| α-helix | 382-393 | 12 | |
| β-strand | 398-399 | 2 | 21 |
| β-strand | 405-406 | 2 | 21 |
| β-strand | 411-414 | 4 | 22 |
| α-helix | 423-432 | 10 | |
| β-strand | 436-438 | 3 | 22 |
| β-strand | 451-454 | 4 | 23 |
| β-strand | 463-466 | 4 | 23 |
| α-helix | 468-471 | 4 | |
| β-strand | 474-479 | 6 | 22 |
| α-helix | 491-499 | 9 | |
| β-strand | 501-506 | 6 | 24 |
| β-strand | 509-514 | 6 | 24 |
| β-strand | 517-522 | 6 | 22 |
| α-helix | 545-547 | 3 | |
| β-strand | 552-554 | 3 | 22 |
| α-helix | 563-576 | 14 | |
| α-helix | 596-609 | 14 | |
| β-strand | 613-614 | 2 | 25 |
| α-helix | 616-635 | 20 | |
| α-helix | 650-665 | 16 | |
| β-strand | 671-672 | 2 | 25 |
| α-helix | 674-685 | 12 | |
Chain 6: 16 helices, 18 β-strands
| Element | Residues | Length | Sheet |
|---|
| α-helix | 501-507 | 7 | |
| α-helix | 510-521 | 12 | |
| α-helix | 525-532 | 8 | |
| α-helix | 541-552 | 12 | |
| β-strand | 557-558 | 2 | 1 |
| β-strand | 564-565 | 2 | 1 |
| β-strand | 571-575 | 5 | 2 |
| α-helix | 581-589 | 9 | |
| β-strand | 596 | 1 | 2 |
| β-strand | 599 | 1 | 3 |
| β-strand | 603 | 1 | 4 |
| β-strand | 610-614 | 5 | 5 |
| β-strand | 621-625 | 5 | 5 |
| β-strand | 635-638 | 4 | 2 |
| β-strand | 639 | 1 | 3 |
| α-helix | 641-643 | 3 | |
| α-helix | 646-653 | 8 | |
| β-strand | 661-663 | 3 | 6 |
| β-strand | 664 | 1 | 7 |
| β-strand | 670-672 | 3 | 6 |
| β-strand | 677-682 | 6 | 2 |
| α-helix | 683-684 | 2 | |
| α-helix | 695-698 | 4 | |
| β-strand | 699 | 1 | 8 |
| α-helix | 703-707 | 5 | |
| β-strand | 711-715 | 5 | 2 |
| α-helix | 721-737 | 17 | |
| α-helix | 738-740 | 3 | |
| α-helix | 748-758 | 11 | |
| β-strand | 764-765 | 2 | 9 |
| α-helix | 767-782 | 16 | |
| α-helix | 798-813 | 16 | |
| β-strand | 818-819 | 2 | 9 |
| α-helix | 821-834 | 14 | |
Chain 7: 18 helices, 14 β-strands
| Element | Residues | Length | Sheet |
|---|
| α-helix | 395-407 | 13 | |
| α-helix | 410-417 | 8 | |
| α-helix | 426-437 | 12 | |
| β-strand | 442-443 | 2 | 10 |
| β-strand | 449-450 | 2 | 10 |
| α-helix | 453-455 | 3 | |
| β-strand | 456-460 | 5 | 11 |
| α-helix | 467-476 | 10 | |
| β-strand | 481-484 | 4 | 11 |
| β-strand | 488 | 1 | 12 |
| α-helix | 490-494 | 5 | |
| β-strand | 495-498 | 4 | 13 |
| β-strand | 507-510 | 4 | 13 |
| α-helix | 512-515 | 4 | |
| β-strand | 519-524 | 6 | 11 |
| α-helix | 526-528 | 3 | |
| α-helix | 531-534 | 4 | |
| α-helix | 538-541 | 4 | |
| β-strand | 546-550 | 5 | 14 |
| β-strand | 553-557 | 5 | 14 |
| β-strand | 561-567 | 7 | 11 |
| α-helix | 580-584 | 5 | |
| α-helix | 588-591 | 4 | |
| β-strand | 596-600 | 5 | 11 |
| α-helix | 606-621 | 16 | |
| α-helix | 635-645 | 11 | |
| β-strand | 651 | 1 | 15 |
| α-helix | 654-673 | 20 | |
| α-helix | 677-679 | 3 | |
| α-helix | 686-702 | 17 | |
| β-strand | 707 | 1 | 15 |
| α-helix | 710-728 | 19 | |
Molecules and chains
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|
| DNA replication licensing factor MCM6 | 6 | protein | 1017 | Saccharomyces cerevisiae (strain ATCC 204508 / S288c) | P53091 (AlphaFold model) |
| DNA replication licensing factor MCM7 | 7 | protein | 845 | Saccharomyces cerevisiae (strain ATCC 204508 / S288c) | P38132 (AlphaFold model) |
| DNA replication licensing factor MCM2 | 2 | protein | 868 | Saccharomyces cerevisiae (strain ATCC 204508 / S288c) | P29469 (AlphaFold model) |
| Minichromosome maintenance protein 5 | 5 | protein | 775 | Saccharomyces cerevisiae (strain ATCC 204508 / S288c) | P29496 (AlphaFold model) |
| DNA replication licensing factor MCM3 | 3 | protein | 971 | Saccharomyces cerevisiae (strain ATCC 204508 / S288c) | P24279 |
| DNA replication licensing factor MCM4 | 4 | protein | 933 | Saccharomyces cerevisiae (strain ATCC 204508 / S288c) | P30665 |
| ssDNA, leading-strand template | I | DNA | 85 | synthetic construct | |
Sequence of entity 1 (6), FASTA
>6SKO_1 DNA replication licensing factor MCM6 (chains 6)
MSSPFPADTPSSNRPSNSSPPPSSIGAGFGSSSGLDSQIGSRLHFPSSSQPHVSNSQTGP
FVNDSTQFSSQRLQTDGSATNDMEGNEPARSFKSRALNHVKKVDDVTGEKVREAFEQFLE
DFSVQSTDTGEVEKVYRAQIEFMKIYDLNTIYIDYQHLSMRENGALAMAISEQYYRFLPF
LQKGLRRVVRKYAPELLNTSDSLKRSEGDEGQADEDEQQDDDMNGSSLPRDSGSSAAPGN
GTSAMATRSITTSTSPEQTERVFQISFFNLPTVHRIRDIRSEKIGSLLSISGTVTRTSEV
RPELYKASFTCDMCRAIVDNVEQSFKYTEPTFCPNPSCENRAFWTLNVTRSRFLDWQKVR
IQENANEIPTGSMPRTLDVILRGDSVERAKPGDRCKFTGVEIVVPDVTQLGLPGVKPSST
LDTRGISKTTEGLNSGVTGLRSLGVRDLTYKISFLACHVISIGSNIGASSPDANSNNRET
ELQMAANLQANNVYQDNERDQEVFLNSLSSDEINELKEMVKDEHIYDKLVRSIAPAVFGH
EAVKKGILLQMLGGVHKSTVEGIKLRGDINICVVGDPSTSKSQFLKYVVGFAPRSVYTSG
KASSAAGLTAAVVRDEEGGDYTIEAGALMLADNGICCIDEFDKMDISDQVAIHEAMEQQT
ISIAKAGIHATLNARTSILAAANPVGGRYNRKLSLRGNLNMTAPIMSRFDLFFVILDDCN
EKIDTELASHIVDLHMKRDEAIEPPFSAEQLRRYIKYARTFKPILTKEARSYLVEKYKEL
RKDDAQGFSRSSYRITVRQLESMIRLSEAIARANCVDEITPSFIAEAYDLLRQSIIRVDV
DDVEMDEEFDNIESQSHAASGNNDDNDDGTGSGVITSEPPADIEEGQSEATARPGTSEKK
KTTVTYDKYVSMMNMIVRKIAEVDREGAEELTAVDIVDWYLLQKENDLGSLAEYWEERRL
AFKVIKRLVKDRILMEIHGTRHNLRDLENEENENNKTVYVIHPNCEVLDQLEPQDSS
Sequence of entity 2 (7), FASTA
>6SKO_2 DNA replication licensing factor MCM7 (chains 7)
MSAALPSIQLPVDYNNLFNEITDFLVTFKQDTLSSDATRNENEDENLDAENIEQHLLEKG
PKYMAMLQKVANRELNSVIIDLDDILQYQNEKFLQGTQADDLVSAIQQNANHFTELFCRA
IDNNMPLPTKEIDYKDDVLDVILNQRRLRNERMLSDRTNEIRSENLMDTTMDPPSSMNDA
LREVVEDETELFPPNLTRRYFLYFKPLSQNCARRYRKKAISSKPLSVRQIKGDFLGQLIT
VRGIITRVSDVKPAVEVIAYTCDQCGYEVFQEVNSRTFTPLSECTSEECSQNQTKGQLFM
STRASKFSAFQECKIQELSQQVPVGHIPRSLNIHVNGTLVRSLSPGDIVDVTGIFLPAPY
TGFKALKAGLLTETYLEAQFVRQHKKKFASFSLTSDVEERVMELITSGDVYNRLAKSIAP
EIYGNLDVKKALLLLLVGGVDKRVGDGMKIRGDINVCLMGDPGVAKSQLLKAICKISPRG
VYTTGKGSSGVGLTAAVMKDPVTDEMILEGGALVLADNGICCIDEFDKMDESDRTAIHEV
MEQQTISISKAGINTTLNARTSILAAANPLYGRYNPRLSPLDNINLPAALLSRFDILFLM
LDIPSRDDDEKLAEHVTYVHMHNKQPDLDFTPVEPSKMREYIAYAKTKRPVMSEAVNDYV
VQAYIRLRQDSKREMDSKFSFGQATPRTLLGIIRLSQALAKLRLADMVDIDDVEEALRLV
RVSKESLYQETNKSKEDESPTTKIFTIIKKMLQETGKNTLSYENIVKTVRLRGFTMLQLS
NCIQEYSYLNVWHLINEGNTLKFVDDGTMDTDQEDSLVSTPKLAPQTTASANVSAQDSDI
DLQDA
Sequence of entity 3 (2), FASTA
>6SKO_3 DNA replication licensing factor MCM2 (chains 2)
MSDNRRRRREEDDSDSENELPPSSPQQHFRGGMNPVSSPIGSPDMINPEGDDNEVDDVPD
IDEVEEQMNEVDLMDDNMYEDYAADHNRDRYDPDQVDDREQQELSLSERRRIDAQLNERD
RLLRNVAYIDDEDEEQEGAAQLDEMGLPVQRRRRRRQYEDLENSDDDLLSDMDIDPLREE
LTLESLSNVKANSYSEWITQPNVSRTIARELKSFLLEYTDETGRSVYGARIRTLGEMNSE
SLEVNYRHLAESKAILALFLAKCPEEMLKIFDLVAMEATELHYPDYARIHSEIHVRISDF
PTIYSLRELRESNLSSLVRVTGVVTRRTGVFPQLKYVKFNCLKCGSILGPFFQDSNEEIR
ISFCTNCKSKGPFRVNGEKTVYRNYQRVTLQEAPGTVPPGRLPRHREVILLADLVDVSKP
GEEVEVTGIYKNNYDGNLNAKNGFPVFATIIEANSIKRREGNTANEGEEGLDVFSWTEEE
EREFRKISRDRGIIDKIISSMAPSIYGHRDIKTAVACSLFGGVPKNVNGKHSIRGDINVL
LLGDPGTAKSQILKYVEKTAHRAVFATGQGASAVGLTASVRKDPITKEWTLEGGALVLAD
KGVCLIDEFDKMNDQDRTSIHEAMEQQSISISKAGIVTTLQARCSIIAAANPNGGRYNST
LPLAQNVSLTEPILSRFDILCVVRDLVDEEADERLATFVVDSHVRSHPENDEDREGEELK
NNGESAIEQGEDEINEQLNARQRRLQRQRKKEEEISPIPQELLMKYIHYARTKIYPKLHQ
MDMDKVSRVYADLRRESISTGSFPITVRHLESILRIAESFAKMRLSEFVSSYDLDRAIKV
VVDSFVDAQKVSVRRQLRRSFAIYTLGH
Sequence of entity 4 (5), FASTA
>6SKO_4 Minichromosome maintenance protein 5 (chains 5)
MSFDRPEIYSAPVLQGESPNDDDNTEIIKSFKNFILEFRLDSQFIYRDQLRNNILVKNYS
LTVNMEHLIGYNEDIYKKLSDEPSDIIPLFETAITQVAKRISILSRAQSANNNDKDPENT
SMDTDSLLLNSLPTFQLILNSNANQIPLRDLDSEHVSKIVRLSGIIISTSVLSSRATYLS
IMCRNCRHTTSITINNFNSITGNTVSLPRSCLSTIESESSMANESNIGDESTKKNCGPDP
YIIIHESSKFIDQQFLKLQEIPELVPVGEMPRNLTMTCDRYLTNKVIPGTRVTIVGIYSI
YNSKNGAGSGRSGGGNGGSGVAIRTPYIKILGIQSDVETSSIWNSVTMFTEEEEEEFLQL
SRNPKLYEILTNSIAPSIFGNEDIKKAIVCLLMGGSKKILPDGMRLRGDINVLLLGDPGT
AKSQLLKFVEKVSPIAVYTSGKGSSAAGLTASVQRDPMTREFYLEGGAMVLADGGVVCID
EFDKMRDEDRVAIHEAMEQQTISIAKAGITTVLNSRTSVLAAANPIYGRYDDLKSPGDNI
DFQTTILSRFDMIFIVKDDHNEERDISIANHVINIHTGNANAMQNQQEENGSEISIEKMK
RYITYCRLKCAPRLSPQAAEKLSSNFVTIRKQLLINELESTERSSIPITIRQLEAIIRIT
ESLAKLELSPIAQERHVDEAIRLFQASTMDAASQDPIGGLNQASGTSLSEIRRFEQELKR
RLPIGWSTSYQTLRREFVDTHRFSQLALDKALYALEKHETIQLRHQGQNIYRSGV
Sequence of entity 5 (3), FASTA
>6SKO_5 DNA replication licensing factor MCM3 (chains 3)
MEGSTGFDGDATTFFAPDAVFGDRVRRFQEFLDTFTSYRDSVRSIQVYNSNNAANYNDDQ
DDADERDLLGDDDGDDLEKEKKAASSTSLNILPHRIIISLDDLREFDRSFWSGILVEPAY
FIPPAEKALTDLADSMDDVPHPNASAVSSRHPWKLSFKGSFGAHALSPRTLTAQHLNKLV
SVEGIVTKTSLVRPKLIRSVHYAAKTGRFHYRDYTDATTTLTTRIPTPAIYPTEDTEGNK
LTTEYGYSTFIDHQRITVQEMPEMAPAGQLPRSIDVILDDDLVDKTKPGDRVNVVGVFKS
LGAGGMNQSNSNTLIGFKTLILGNTVYPLHARSTGVAARQMLTDFDIRNINKLSKKKDIF
DILSQSLAPSIYGHDHIKKAILLMLMGGVEKNLENGSHLRGDINILMVGDPSTAKSQLLR
FVLNTASLAIATTGRGSSGVGLTAAVTTDRETGERRLEAGAMVLADRGVVCIDEFDKMTD
VDRVAIHEVMEQQTVTIAKAGIHTTLNARCSVIAAANPVFGQYDVNRDPHQNIALPDSLL
SRFDLLFVVTDDINEIRDRSISEHVLRTHRYLPPGYLEGEPVRERLNLSLAVGEDADINP
EEHSNSGAGVENEGEDDEDHVFEKFNPLLQAGAKLAKNKGNYNGTEIPKLVTIPFLRKYV
QYAKERVIPQLTQEAINVIVKNYTDLRNDDNTKKSPITARTLETLIRLATAHAKVRLSKT
VNKVDAKVAANLLRFALLGEDIGNDIDEEESEYEEALSKRSPQKSPKKRQRVRQPASNSG
SPIKSTPRRSTASSVNATPSSARRILRFQDDEQNAGEDDNDIMSPLPADEEAELQRRLQL
GLRVSPRRREHLHAPEEGSSGPLTEVGTPRLPNVSSAGQDDEQQQSVISFDNVEPGTIST
GRLSLISGIIARLMQTEIFEEESYPVASLFERINEELPEEEKFSAQEYLAGLKIMSDRNN
LMVADDKVWRV
Sequence of entity 6 (4), FASTA
>6SKO_6 DNA replication licensing factor MCM4 (chains 4)
MSQQSSSPTKEDNNSSSPVVPNPDSVPPQLSSPALFYSSSSSQGDIYGRNNSQNLSQGEG
NIRAAIGSSPLNFPSSSQRQNSDVFQSQGRQGRIRSSASASGRSRYHSDLRSDRALPTSS
SSLGRNGQNRVHMRRNDIHTSDLSSPRRIVDFDTRSGVNTLDTSSSSAPPSEASEPLRII
WGTNVSIQECTTNFRNFLMSFKYKFRKILDEREEFINNTTDEELYYIKQLNEMRELGTSN
LNLDARNLLAYKQTEDLYHQLLNYPQEVISIMDQTIKDCMVSLIVDNNLDYDLDEIETKF
YKVRPYNVGSCKGMRELNPNDIDKLINLKGLVLRSTPVIPDMKVAFFKCNVCDHTMAVEI
DRGVIQEPARCERIDCNEPNSMSLIHNRCSFADKQVIKLQETPDFVPDGQTPHSISLCVY
DELVDSCRAGDRIEVTGTFRSIPIRANSRQRVLKSLYKTYVDVVHVKKVSDKRLDVDTST
IEQELMQNKVDHNEVEEVRQITDQDLAKIREVAAREDLYSLLARSIAPSIYELEDVKKGI
LLQLFGGTNKTFTKGGRYRGDINILLCGDPSTSKSQILQYVHKITPRGVYTSGKGSSAVG
LTAYITRDVDTKQLVLESGALVLSDGGVCCIDEFDKMSDSTRSVLHEVMEQQTISIAKAG
IITTLNARSSILASANPIGSRYNPNLPVTENIDLPPPLLSRFDLVYLVLDKVDEKNDREL
AKHLTNLYLEDKPEHISQDDVLPVEFLTMYISYAKEHIHPIITEAAKTELVRAYVGMRKM
GDDSRSDEKRITATTRQLESMIRLAEAHAKMKLKNVVELEDVQEAVRLIRSAIKDYATDP
KTGKIDMNLVQTGKSVIQRKLQEDLSREIMNVLKDQASDSMSFNELIKQINEHSQDRVES
SDIQEALSRLQQEDKVIVLGEGVRRSVRLNNRV
Sequence of entity 7 (I), FASTA
>6SKO_7 ssDNA, leading-strand template (chains I)
TAGAGTAGGAAGTGATGGTAAGTGATTAGAGAATTGGAGAGTGTGTTTTTTTTTTTTTTT
TTTTTTTTTTTTTTTTTTTTTTTTT
Ligands and cofactors
| ID | Name | Formula | Copies |
|---|
| ANP | Phosphoaminophosphonic acid-adenylate ester | C10 H17 N6 O12 P3 | 5 |
| MG | Magnesium ion | Mg | 5 |
Primary citation
Cryo-EM Structure of the Fork Protection Complex Bound to CMG at a Replication Fork. Baretic, D., Jenkyn-Bedford, M., Aria, V. et al. Mol Cell (2020) 78:926-940.e13. DOI 10.1016/j.molcel.2020.04.012 · PubMed
Other PDB entries of the same protein (UniProt P53091 (AlphaFold model), which also has an AlphaFold model), best resolution first:
- 7W8G 2.52 Å, Cryo-EM structure of MCM double hexamer
- 28VY 2.7 Å, sCMGE assembled on ARS1 DNA with Sld2 and RPA
- 8RIF 2.79 Å, Cryo-EM structure of the MCM double hexamer loaded onto dsDNA.
- 7V3V 2.9 Å, Cryo-EM structure of MCM double hexamer bound with DDK in State I
- 9TH8 2.9 Å, Cryo-EM structure of MCM2-7 DH bound to Sld3-Sld7, Cdc45 and DNA
- 7P30 3.0 Å, 3.0 A resolution structure of a DNA-loaded MCM double hexamer
- 8KG6 3.07 Å, Yeast replisome in state I
- 9RHL 3.1 Å, Phospho-DH bound by Sld3-MBD on ARS1 DNA
- 7PMK 3.2 Å, S. cerevisiae replisome-SCF(Dia2) complex bound to double-stranded DNA (conformation I)
- 7PMN 3.2 Å, S. cerevisiae replisome-SCF(Dia2) complex bound to double-stranded DNA (conformation II)
- 7PT6 3.2 Å, Structure of MCM2-7 DH complexed with Cdc7-Dbf4 in the presence of ATPgS, state III
- 7V3U 3.2 Å, Cryo-EM structure of MCM double hexamer with structured Mcm4-NSD
Browse structure collections
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