Structural basis for Scc3-dependent cohesin recruitment to chromatin. Determined by X-ray diffraction at 3.63 Å resolution. Released 29 Aug 2018.
Explore 6H8Q in 3D Show helices and sheets RCSB PDB PDBe
6H8Q contains 112 α-helices and 0 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.
| Element | Residues | Length | Sheet |
|---|---|---|---|
| α-helix | 150-159 | 10 | |
| α-helix | 165-179 | 15 | |
| α-helix | 187-190 | 4 | |
| α-helix | 196-202 | 7 | |
| α-helix | 205-208 | 4 | |
| α-helix | 218-222 | 5 | |
| α-helix | 232-236 | 5 | |
| α-helix | 237-243 | 7 | |
| α-helix | 245-249 | 5 | |
| α-helix | 270-282 | 13 | |
| α-helix | 288-312 | 25 | |
| α-helix | 313-317 | 5 | |
| α-helix | 318-325 | 8 | |
| α-helix | 338-361 | 24 | |
| α-helix | 362-367 | 6 | |
| α-helix | 376-384 | 9 | |
| α-helix | 386-392 | 7 | |
| α-helix | 404-409 | 6 | |
| α-helix | 416-429 | 14 | |
| α-helix | 444-459 | 16 | |
| α-helix | 466-480 | 15 | |
| α-helix | 485-492 | 8 | |
| α-helix | 493-495 | 3 | |
| α-helix | 510-536 | 27 | |
| α-helix | 538-540 | 3 | |
| α-helix | 551-570 | 20 | |
| α-helix | 574-575 | 2 | |
| α-helix | 578-589 | 12 | |
| α-helix | 600-607 | 8 | |
| α-helix | 648-664 | 17 | |
| α-helix | 674-680 | 7 | |
| α-helix | 684-690 | 7 | |
| α-helix | 696-706 | 11 | |
| α-helix | 712-715 | 4 | |
| α-helix | 721-736 | 16 | |
| α-helix | 747-761 | 15 | |
| α-helix | 764-787 | 24 | |
| α-helix | 798-805 | 8 | |
| α-helix | 806-810 | 5 | |
| α-helix | 811-816 | 6 | |
| α-helix | 826-835 | 10 | |
| α-helix | 837-839 | 3 | |
| α-helix | 841-844 | 4 | |
| α-helix | 851-854 | 4 | |
| α-helix | 858-867 | 10 | |
| α-helix | 872-875 | 4 | |
| α-helix | 889-911 | 23 | |
| α-helix | 920-946 | 27 | |
| α-helix | 953-962 | 10 | |
| α-helix | 969-990 | 22 | |
| α-helix | 1002-1005 | 4 | |
| α-helix | 1018-1032 | 15 | |
| α-helix | 1038-1044 | 7 | |
| α-helix | 1053-1060 | 8 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| α-helix | 150-162 | 13 | |
| α-helix | 165-179 | 15 | |
| α-helix | 187-190 | 4 | |
| α-helix | 196-202 | 7 | |
| α-helix | 205-208 | 4 | |
| α-helix | 218-222 | 5 | |
| α-helix | 232-236 | 5 | |
| α-helix | 237-243 | 7 | |
| α-helix | 271-282 | 12 | |
| α-helix | 290-312 | 23 | |
| α-helix | 313-317 | 5 | |
| α-helix | 318-325 | 8 | |
| α-helix | 338-361 | 24 | |
| α-helix | 362-367 | 6 | |
| α-helix | 376-384 | 9 | |
| α-helix | 386-392 | 7 | |
| α-helix | 404-409 | 6 | |
| α-helix | 416-428 | 13 | |
| α-helix | 444-459 | 16 | |
| α-helix | 466-479 | 14 | |
| α-helix | 485-492 | 8 | |
| α-helix | 493-495 | 3 | |
| α-helix | 510-536 | 27 | |
| α-helix | 538-540 | 3 | |
| α-helix | 551-570 | 20 | |
| α-helix | 574-575 | 2 | |
| α-helix | 578-589 | 12 | |
| α-helix | 594-596 | 3 | |
| α-helix | 600-607 | 8 | |
| α-helix | 648-664 | 17 | |
| α-helix | 674-680 | 7 | |
| α-helix | 684-690 | 7 | |
| α-helix | 696-706 | 11 | |
| α-helix | 712-715 | 4 | |
| α-helix | 721-736 | 16 | |
| α-helix | 747-760 | 14 | |
| α-helix | 764-787 | 24 | |
| α-helix | 798-805 | 8 | |
| α-helix | 806-810 | 5 | |
| α-helix | 811-816 | 6 | |
| α-helix | 826-832 | 7 | |
| α-helix | 837-839 | 3 | |
| α-helix | 841-844 | 4 | |
| α-helix | 851-854 | 4 | |
| α-helix | 859-869 | 11 | |
| α-helix | 872-875 | 4 | |
| α-helix | 894-911 | 18 | |
| α-helix | 920-946 | 27 | |
| α-helix | 953-962 | 10 | |
| α-helix | 969-990 | 22 | |
| α-helix | 1002-1005 | 4 | |
| α-helix | 1018-1032 | 15 | |
| α-helix | 1038-1044 | 7 | |
| α-helix | 1053-1059 | 7 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| α-helix | 363-373 | 11 | |
| α-helix | 377-380 | 4 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| α-helix | 364-372 | 9 | |
| α-helix | 378-383 | 6 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| Cohesin subunit SCC3 | A, B | protein | 1150 | Saccharomyces cerevisiae (strain ATCC 204508 / S288c) | P40541 (AlphaFold model) |
| Sister chromatid cohesion protein 1 | G, H | protein | 100 | Saccharomyces cerevisiae (strain ATCC 204508 / S288c) | Q12158 (AlphaFold model) |
| DNA (5'-d(p*cp*tp*tp*tp*cp*gp*tp*tp*tp*cp*cp*tp*tp*gp*ap*ap*ap*ap*a)-3') | E | DNA | 19 | Homo sapiens | |
| DNA (5'-d(p*cp*tp*tp*tp*cp*gp*tp*tp*tp*cp*cp*tp*tp*gp*ap*ap*ap*ap*a)-3') | F | DNA | 19 | Homo sapiens | |
| DNA (5'-d(p*tp*tp*tp*tp*tp*cp*ap*ap*gp*gp*ap*ap*ap*cp*gp*ap*ap*ap*g)-3') | C | DNA | 19 | Homo sapiens | |
| DNA (5'-d(p*cp*tp*tp*tp*cp*gp*tp*tp*tp*cp*cp*tp*tp*gp*ap*ap*ap*ap*a)-3') | D | DNA | 19 | Homo sapiens |
>6H8Q_1 Cohesin subunit SCC3 (chains A, B) MTAVRRSTRIRTKSQVIEEDYDDEQNTSAQHVESDKITAKTQHEEEEEQDTGESEESSSE DDYEDQDDDDYVDTATAKRKSRKRKPKSASNTSSKRQKKKPTSAQKSAVSHAPAYHRSKK DQDQYLEIAKDFQPTELFDILSTSEDVSIEELLREWLETYSENRDKFLQEFINLLLNCCG SVARVEDHDVHSNESSNETIGEIQLLFQRQKLHEFYLLISKENKKRKNFKMGPLYQNFAE FMTKLLEVANDLQLLYVESDEDDTQIVTGNLVLDLLTWLSSFSVCKIRCFRYISTLTLYL FQDYLTQQAVNLEKNYLAKLSKQLSLEEKKKRPNNKTLEKLESTIAETQGSKVVIDSIID NIVKLCFVHRYKDVSDLIRSESMLHLSIWIKNYPEYFLKVTFLKYFGWLLSDNSVSVRLQ VTKILPHLIIQNHNSKSTDNSAIRQVFERFKTKILEVAIRDVNLDVRIHSIQVLTEASSL GYLDDSEILIISSLMFDEEFDPFKTSSFNKRSKFLSTVAKFLARVIKEKFDEFIKTHEDL PKEVDGLEVGPVVQVGIFIKILNDSLIYHLKDCAEVDSRTKIRMLTQAAEFLSPYISTHL KTICNLLISDTESNELIQKLQNSANNNSDDEDVDDEELDITPLFPIDRNSTILYLNVFHG LCAGANNPKIQTKDSVKEIVLPLFYDLLNAASIESADILCPLLESFITFSLDDWISIGYE TELKKITDKTIKAFMDSTIGNSKVDMKYDIFAKFIHHIHHFEKKELQEKFLNQIATLKIH LKKFLQEKMDPNNSRDDYKDLTCSLYELYINKLTILGRDYPIEVDEELLQLFLNNFVSRI PIMFQDFDDSTAQEINFKMLVLLATWNLEKWREIIEKVRDYENSISKDLRSVWKPIAAII GRLNTLVISLAATNETFENINSLFYLKWSACTSLMDIIVAIKIFELKLPADATTWRYSMS EQFPFYLHDNASKVLLKIFLYLESLFAKQVDVQLERVADEDANLNDLPETGFFENIETEF LLFTVKLKGLMKLNILDERFASRVALNKEKLGPLFKKIVDDTIMENPEPNKKNIQKAKSN QTQREKAPLQPNSERETDHANTENNDPDIPMTIDLEPIEESSQNNSELAPIEEHPTVVDA IDNSDEITQD
>6H8Q_2 Sister chromatid cohesion protein 1 (chains G, H) TDAMTESQPKQTGTRRNSKLLNTKSIQIDEETENSESIASSNTYKEERSNNLLTPQPTNF TTKRLWSEITESMSYLPDPILKNFLSYESLKKRKIHNGRE
>6H8Q_3 DNA (5'-D(P*CP*TP*TP*TP*CP*GP*TP*TP*TP*CP*CP*TP*TP*GP*AP*AP*AP*AP*A)-3') (chains E) TTTTCAAGGAAACGAAACG
>6H8Q_4 DNA (5'-D(P*CP*TP*TP*TP*CP*GP*TP*TP*TP*CP*CP*TP*TP*GP*AP*AP*AP*AP*A)-3') (chains F) CGTTTCGTTTCCTTGAAAA
>6H8Q_5 DNA (5'-D(P*TP*TP*TP*TP*TP*CP*AP*AP*GP*GP*AP*AP*AP*CP*GP*AP*AP*AP*G)-3') (chains C) TTTTTCAAGGAAACGAAAG
>6H8Q_6 DNA (5'-D(P*CP*TP*TP*TP*CP*GP*TP*TP*TP*CP*CP*TP*TP*GP*AP*AP*AP*AP*A)-3') (chains D) CTTTCGTTTCCTTGAAAAA
Structural basis for Scc3-dependent cohesin recruitment to chromatin. Li, Y., Muir, K., Bowler, M.W. et al. Elife (2018) 7. DOI 10.7554/eLife.38356 · PubMed
Other PDB entries of the same protein (UniProt P40541 (AlphaFold model), which also has an AlphaFold model), best resolution first:
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