Structural basis of cohesin ring opening. Determined by electron microscopy at 3.3 Å resolution. Released 5 Feb 2020.
Explore 6QPW in 3D Show helices and sheets RCSB PDB PDBe
6QPW contains 28 α-helices and 38 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 |
|---|---|---|---|
| β-strand | 3-10 | 8 | 1 |
| β-strand | 18-22 | 5 | 1 |
| β-strand | 28-32 | 5 | 2 |
| α-helix | 39-49 | 11 | |
| α-helix | 63-65 | 3 | |
| β-strand | 117-124 | 8 | 1 |
| β-strand | 130 | 1 | 1 |
| β-strand | 133-137 | 5 | 1 |
| β-strand | 143-147 | 5 | 1 |
| β-strand | 150-152 | 3 | 1 |
| α-helix | 154-163 | 10 | |
| β-strand | 174-175 | 2 | 2 |
| α-helix | 179-184 | 6 | |
| α-helix | 188-198 | 11 | |
| α-helix | 205-233 | 29 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| α-helix | 484-498 | 15 | |
| β-strand | 501-503 | 3 | 3 |
| α-helix | 504-512 | 9 | |
| α-helix | 516-518 | 3 | |
| β-strand | 520 | 1 | 4 |
| α-helix | 521-536 | 16 | |
| β-strand | 540-543 | 4 | 3 |
| β-strand | 552-555 | 4 | 3 |
| α-helix | 557-560 | 4 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| β-strand | 3-9 | 7 | 5 |
| β-strand | 14 | 1 | 6 |
| β-strand | 18-20 | 3 | 5 |
| β-strand | 27-31 | 5 | 6 |
| α-helix | 42-45 | 4 | |
| α-helix | 58-64 | 7 | |
| β-strand | 68 | 1 | 7 |
| β-strand | 71 | 1 | 7 |
| β-strand | 76 | 1 | 8 |
| β-strand | 77-82 | 6 | 5 |
| β-strand | 109 | 1 | 8 |
| α-helix | 125-133 | 9 | |
| α-helix | 159-170 | 12 | |
| α-helix | 172-174 | 3 | |
| α-helix | 177-203 | 27 | |
| α-helix | 1013-1059 | 47 | |
| β-strand | 1065 | 1 | 9 |
| β-strand | 1113 | 1 | 9 |
| β-strand | 1121 | 1 | 9 |
| α-helix | 1128-1142 | 15 | |
| β-strand | 1150-1154 | 5 | 6 |
| α-helix | 1162-1175 | 14 | |
| β-strand | 1180-1184 | 5 | 6 |
| α-helix | 1188-1190 | 3 | |
| β-strand | 1196-1202 | 7 | 6 |
| β-strand | 1207-1210 | 4 | 6 |
| α-helix | 1216-1220 | 5 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| α-helix | 1070-1125 | 56 | |
| β-strand | 1135-1140 | 6 | 10 |
| α-helix | 1147-1149 | 3 | |
| β-strand | 1152-1157 | 6 | 10 |
| α-helix | 1166-1168 | 3 | |
| α-helix | 1171-1186 | 16 | |
| β-strand | 1193-1196 | 4 | 2 |
| α-helix | 1205-1218 | 14 | |
| β-strand | 1220 | 1 | 11 |
| β-strand | 1223 | 1 | 11 |
| β-strand | 1224-1228 | 5 | 2 |
| α-helix | 1232-1235 | 4 | |
| β-strand | 1240-1247 | 8 | 2 |
| β-strand | 1252-1259 | 8 | 2 |
| β-strand | 1264 | 1 | 4 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| Structural maintenance of chromosomes protein,Structural maintenance of chromosomes protein | A | protein | 242 | Chaetomium thermophilum var. thermophilum DSM 1495 | G0SGH3 (AlphaFold model) |
| Sister chromatid cohesion protein 1 | B | protein | 85 | Saccharomyces cerevisiae S288C | Q12158 (AlphaFold model) |
| Structural maintenance of chromosomes protein 3,Structural maintenance of chromosomes protein 3 | C | protein | 535 | Saccharomyces cerevisiae S288C | P47037 (AlphaFold model) |
| Sister chromatid cohesion protein 1,Structural maintenance of chromosomes protein | E | protein | 372 | Saccharomyces cerevisiae S288C, Chaetomium thermophilum var. thermophilum DSM 1495 | G0SGH3 (AlphaFold model), Q12158 (AlphaFold model) |
>6QPW_1 Structural maintenance of chromosomes protein,Structural maintenance of chromosomes protein (chains A) MGKLIRLELFNFKSYKGHHTLLFGDSYFTSIIGPNGSGKSNSMDAISFVLGIKSSHLRSS NLRDLIYRGRVMKTSKIQDDGTTAPATNGDVNGYENGDAGDDEDTSQRTSRNDPKTAWVM AVYEDDAGELHRWKRTITANGTSEYRINDRVVNAQQYNEALEKENILIKARNFLVFQGDV EAIASQSPQDLTRLIEQISGSLEYKEEYERLEEEVRQATEEQAYKLQRRRAANSEIKQYM EQ
>6QPW_2 Sister chromatid cohesion protein 1 (chains B) MASKAIVQMAKILRKELSEEKEVIFTDVLKSQANTEPENITKREASRGFFDILSLATEGC IGLSQTEAFGNIKIDAKPALFERFI
>6QPW_3 Structural maintenance of chromosomes protein 3,Structural maintenance of chromosomes protein 3 (chains C) MAYIKRVIIKGFKTYRNETIIDNFSPHQNVIIGSNGSGKSNFFAAIRFVLSDDYSNLKRE ERQGLIHQGSGGSVMSASVEIVFHDPDHSMILPSGVLSRGDDEVTIRRTVGLKKDDYQLN DRNVTKGDIVRMLETAGFSMNNPYNIVPQGKIVALTNAKDKERLQLLEDVVGAKSFEVKL KASLKKMEETEQKKIQINKEMGELNSKLSEMEQERKELEKYNELERNRKIYQFTLYDREL NEVINQMERLDGDYNNTVYSSESSKHPTSLVPRGSDITSDQLLQRLNDMNTEISGLKNVN KRAFENFKKFNERRKDLAERASELDESKDSIQDLIVKLKQQKVNAVDSTFQKVSENFEAV FERLVPRGTAKLIIHRKNDNANDHDESIDVDMDAESNESQNGKDSEIMYTGVSISVSFNS KQNEQLHVEQLSGGQKTVCAIALILAIQMVDPASFYLFDEIDACLDKQYRTAVATLLKEL SKNAQFICTTFRTDMLQVADKFFRVKYECKISTVIEVNREEAIGFIRGSNKFAEV
>6QPW_4 Sister chromatid cohesion protein 1,Structural maintenance of chromosomes protein (chains E) MVTENPQRLTVLRLATNKGPLAQIWLASNMSNIPRGSVIQTHIAESAKEIAKASGSDDES GDNEYITLRTSGELLQGIVRVYSKQATFLLTDIKDTLTKISMLFKTSQKMTSTVNRLNTV TRVHQLMLEDAVTEREVLVTPGLEFLDDTTIPVGLMAQENPNLRAMDRLDHVRKQLEQTE QEFEASKAKLRQARESFQAVKQKRLELFNKAFTHIQEQITHVYKELTRSEAYPLGGQAYL DIEEDTDTPFLSGVKYHAMPPCKRFRDMEHLSGGEKTMAALALLFAIHSYQPSPFFVLDE VDCALDNANVEKIKKYIREHAGPGMQFIVISLKPALFQASESLIGVYRDQEANTSRTLTL DLRKYRHHHHHH
| ID | Name | Formula | Copies |
|---|---|---|---|
| AGS | Phosphothiophosphoric acid-adenylate ester | C10 H16 N5 O12 P3 S | 2 |
| MG | Magnesium ion | Mg | 2 |
The structure of the cohesin ATPase elucidates the mechanism of SMC-kleisin ring opening. Muir, K.W., Li, Y., Weis, F. et al. Nat Struct Mol Biol (2020) 27:233-239. DOI 10.1038/s41594-020-0379-7 · PubMed
Other PDB entries of the same protein (UniProt G0SGH3 (AlphaFold model), which also has an AlphaFold model), best resolution first:
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