Folded elbow of cohesin. Determined by electron microscopy at 5.5 Å resolution. Released 28 Jul 2021.
Explore 7OGT in 3D Show helices and sheets RCSB PDB PDBe
7OGT contains 32 α-helices and 18 β-strands across 2 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 | 248-373 | 126 | |
| α-helix | 382-525 | 144 | |
| β-strand | 531-532 | 2 | 1 |
| α-helix | 534-536 | 3 | |
| α-helix | 545-556 | 12 | |
| β-strand | 559-561 | 3 | 1 |
| α-helix | 564-577 | 14 | |
| β-strand | 581-586 | 6 | 1 |
| α-helix | 590-593 | 4 | |
| β-strand | 607 | 1 | 2 |
| α-helix | 608-611 | 4 | |
| α-helix | 616-626 | 11 | |
| β-strand | 630-632 | 3 | 2 |
| α-helix | 635-642 | 8 | |
| β-strand | 651-653 | 3 | 2 |
| β-strand | 658-659 | 2 | 2 |
| β-strand | 665-666 | 2 | 2 |
| α-helix | 678-786 | 109 | |
| α-helix | 798-801 | 4 | |
| α-helix | 806-942 | 137 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| α-helix | 238-394 | 157 | |
| α-helix | 403-409 | 7 | |
| α-helix | 410-414 | 5 | |
| α-helix | 415-450 | 36 | |
| α-helix | 457-508 | 52 | |
| α-helix | 513-526 | 14 | |
| α-helix | 540-543 | 4 | |
| β-strand | 544-546 | 3 | 3 |
| α-helix | 548-550 | 3 | |
| α-helix | 551-558 | 8 | |
| α-helix | 559-563 | 5 | |
| β-strand | 565-567 | 3 | 4 |
| α-helix | 570-579 | 10 | |
| β-strand | 589 | 1 | 2 |
| β-strand | 590-592 | 3 | 4 |
| α-helix | 605-607 | 3 | |
| β-strand | 615-616 | 2 | 5 |
| α-helix | 617-620 | 4 | |
| β-strand | 621-623 | 3 | 3 |
| α-helix | 625-627 | 3 | |
| α-helix | 628-635 | 8 | |
| β-strand | 638-641 | 4 | 5 |
| α-helix | 644-653 | 10 | |
| β-strand | 657-660 | 4 | 5 |
| β-strand | 666 | 1 | 1 |
| β-strand | 672-675 | 4 | 1 |
| α-helix | 683-790 | 108 | |
| α-helix | 799-829 | 31 | |
| α-helix | 830-834 | 5 | |
| α-helix | 835-951 | 117 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| Structural maintenance of chromosomes protein 1 | A | protein | 1225 | Saccharomyces cerevisiae (strain ATCC 204508 / S288c) | P32908 (AlphaFold model) |
| Structural maintenance of chromosomes protein 3 | B | protein | 1230 | Saccharomyces cerevisiae (strain ATCC 204508 / S288c) | P47037 (AlphaFold model) |
>7OGT_1 Structural maintenance of chromosomes protein 1 (chains A) MGRLVGLELSNFKSYRGVTKVGFGESNFTSIIGPNGSGKSNMMDAISFVLGVRSNHLRSN ILKDLIYRGVLNDENSDDYDNEGAASSNPQSAYVKAFYQKGNKLVELMRIISRNGDTSYK IDGKTVSYKDYSIFLENENILIKAKNFLVFQGDVEQIAAQSPVELSRMFEEVSGSIQYKK EYEELKEKIEKLSKSATESIKNRRRIHGELKTYKEGINKNEEYRKQLDKKNELQKFQALW QLYHLEQQKEELTDKLSALNSEISSLKGKINNEMKSLQRSKSSFVKESAVISKQKSKLDY IFKDKEKLVSDLRLIKVPQQAAGKRISHIEKRIESLQKDLQRQKTYVERFETQLKVVTRS KEAFEEEIKQSARNYDKFKLNENDLKTYNCLHEKYLTEGGSILEEKIAVLNNDKREIQEE LERFNKRADISKRRITEELSITGEKLDTQLNDLRVSLNEKNALHTERLHELKKLQSDIES ANNQEYDLNFKLRETLVKIDDLSANQRETMKERKLRENIAMLKRFFPGVKGLVHDLCHPK KEKYGLAVSTILGKNFDSVIVENLTVAQECIAFLKKQRAGTASFIPLDTIETELPTLSLP DSQDYILSINAIDYEPEYEKAMQYVCGDSIICNTLNIAKDLKWKKGIRGKLVTIEGALIH KAGLMTGGISGDANNRWDKEEYQSLMSLKDKLLIQIDELSNGQRSNSIRAREVENSVSLL NSDIANLRTQVTQQKRSLDENRLEIKYHNDLIEKEIQPKITELKKKLDDLENTKDNLVKE KEALQNNIFKEFTSKIGFTIKEYENHSGELMRQQSKELQQLQKQILTVENKLQFETDRLS TTQRRYEKAQKDLENAQVEMKSLEEQEYAIEMKIGSIESKLEEHKNHLDELQKKFVTKQS ELNSSEDILEDMNSNLQVLKRERDGIKEDIEKFDLERVTALKNCKISNINIPISSETTID DLPISSTDNEAITISNSIDINYKGLPKKYKENNTDSARKELEQKIHEVEEILNELQPNAR ALERYDEAEGRFEVINNETEQLKAEEKKILNQFLKIKKKRKELFEKTFDYVSDHLDAIYR ELTKNPNSNVELAGGNASLTIEDEDEPFNAGIKYHATPPLKRFKDMEYLSGGEKTVAALA LLFAINSYQPSPFFVLDEVDAALDITNVQRIAAYIRRHRNPDLQFIVISLKNTMFEKSDA LVGVYRQQQENSSKIITLDLSNYAE
>7OGT_2 Structural maintenance of chromosomes protein 3 (chains B) MYIKRVIIKGFKTYRNETIIDNFSPHQNVIIGSNGSGKSNFFAAIRFVLSDDYSNLKREE RQGLIHQGSGGSVMSASVEIVFHDPDHSMILPSGVLSRGDDEVTIRRTVGLKKDDYQLND RNVTKGDIVRMLETAGFSMNNPYNIVPQGKIVALTNAKDKERLQLLEDVVGAKSFEVKLK ASLKKMEETEQKKIQINKEMGELNSKLSEMEQERKELEKYNELERNRKIYQFTLYDRELN EVINQMERLDGDYNNTVYSSEQYIQELDKREDMIDQVSKKLSSIEASLKIKNATDLQQAK LRESEISQKLTNVNVKIKDVQQQIESNEEQRNLDSATLKEIKSIIEQRKQKLSKILPRYQ ELTKEEAMYKLQLASLQQKQRDLILKKGEYARFKSKDERDTWIHSEIEELKSSIQNLNEL ESQLQMDRTSLRKQYSAIDEEIEELIDSINGPDTKGQLEDFDSELIHLKQKLSESLDTRK ELWRKEQKLQTVLETLLSDVNQNQRNVNETMSRSLANGIINVKEITEKLKISPESVFGTL GELIKVNDKYKTCAEVIGGNSLFHIVVDTEETATLIMNELYRMKGGRVTFIPLNRLSLDS DVKFPSNTTTQIQFTPLIKKIKYEPRFEKAVKHVFGKTIVVKDLGQGLKLAKKHKLNAIT LDGDRADKRGVLTGGYLDQHKRTRLESLKNLNESRSQHKKILEELDFVRNELNDIDTKID QVNGNIRKVSNDRESVLTNIEVYRTSLNTKKNEKLILEESLNAIILKLEKLNTNRTFAQE KLNTFENDLLQEFDSELSKEEKERLESLTKEISAAHNKLNITSDALEGITTTIDSLNAEL ESKLIPQENDLESKMSEVGDAFIFGLQDELKELQLEKESVEKQHENAVLELGTVQREIES LIAEETNNKKLLEKANNQQRLLLKKLDNFQKSVEKTMIKKTTLVTRREELQQRIREIGLL PEDALVNDFSDITSDQLLQRLNDMNTEISGLKNVNKRAFENFKKFNERRKDLAERASELD ESKDSIQDLIVKLKQQKVNAVDSTFQKVSENFEAVFERLVPRGTAKLIIHRKNDNANDHD ESIDVDMDAESNESQNGKDSEIMYTGVSISVSFNSKQNEQLHVEQLSGGQKTVCAIALIL AIQMVDPASFYLFDEIDAALDKQYRTAVATLLKELSKNAQFICTTFRTDMLQVADKFFRV KYENKISTVIEVNREEAIGFIRGSNKFAEV
Folding of cohesin's coiled coil is important for Scc2/4-induced association with chromosomes. Petela, N.J., Gonzalez Llamazares, A., Dixon, S. et al. Elife (2021) 10. DOI 10.7554/eLife.67268 · PubMed
Other PDB entries of the same protein (UniProt P32908 (AlphaFold model), which also has an AlphaFold model), best resolution first:
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