Crystal structure of the central region of human cohesin subunit STAG1 in complex with RAD21 peptide. Determined by X-ray diffraction at 3.17 Å resolution. Released 26 Jun 2019.
Explore 6RRK in 3D Show helices and sheets RCSB PDB PDBe
6RRK contains 56 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 | 462-473 | 12 | |
| α-helix | 481-487 | 7 | |
| α-helix | 493-496 | 4 | |
| α-helix | 499-507 | 9 | |
| α-helix | 516-518 | 3 | |
| α-helix | 519-538 | 20 | |
| α-helix | 554-581 | 28 | |
| α-helix | 586-592 | 7 | |
| α-helix | 596-598 | 3 | |
| α-helix | 603-606 | 4 | |
| α-helix | 610-626 | 17 | |
| α-helix | 630-643 | 14 | |
| α-helix | 651-677 | 27 | |
| α-helix | 685-704 | 20 | |
| α-helix | 712-725 | 14 | |
| α-helix | 731-753 | 23 | |
| α-helix | 759-779 | 21 | |
| α-helix | 785-801 | 17 | |
| α-helix | 804-807 | 4 | |
| α-helix | 820-822 | 3 | |
| α-helix | 823-836 | 14 | |
| α-helix | 856-877 | 22 | |
| α-helix | 883-892 | 10 | |
| α-helix | 897-909 | 13 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| α-helix | 462-473 | 12 | |
| α-helix | 478-480 | 3 | |
| α-helix | 481-487 | 7 | |
| α-helix | 493-496 | 4 | |
| α-helix | 499-507 | 9 | |
| α-helix | 515-518 | 4 | |
| α-helix | 519-538 | 20 | |
| α-helix | 554-581 | 28 | |
| α-helix | 586-592 | 7 | |
| α-helix | 596-598 | 3 | |
| α-helix | 603-606 | 4 | |
| α-helix | 610-625 | 16 | |
| α-helix | 630-643 | 14 | |
| α-helix | 651-676 | 26 | |
| α-helix | 685-704 | 20 | |
| α-helix | 712-725 | 14 | |
| α-helix | 731-754 | 24 | |
| α-helix | 759-779 | 21 | |
| α-helix | 785-801 | 17 | |
| α-helix | 804-806 | 3 | |
| α-helix | 812-814 | 3 | |
| α-helix | 820-822 | 3 | |
| α-helix | 823-836 | 14 | |
| α-helix | 856-877 | 22 | |
| α-helix | 883-892 | 10 | |
| α-helix | 901-909 | 9 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| α-helix | 369-372 | 4 | |
| α-helix | 379-380 | 2 | |
| α-helix | 383-390 | 8 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| Cohesin subunit SA-1 | A, B | protein | 459 | Homo sapiens | Q8WVM7 (AlphaFold model) |
| Double-strand-break repair protein rad21 homolog | C, D | protein | 40 | Homo sapiens | O60216 (AlphaFold model) |
>6RRK_1 Cohesin subunit SA-1 (chains A, B) SMSPNGNLIRMLVLFFLESELHEHAAYLVDSLWESSQELLKDWECMTELLLEEPVQGEEA MSDRQESALIELMVCTIRQAAEAHPPVGRGTGKRVLTAKERKTQIDDRNKLTEHFIITLP MLLSKYSADAEKVANLLQIPQYFDLEIYSTGRMEKHLDALLKQIKFVVEKHVESDVLEAC SKTYSILCSEEYTIQNRVDIARSQLIDEFVDRFNHSVEDLLQEGEEADDDDIYNVLSTLK RLTSFHNAHDLTKWDLFGNCYRLLKTGIEHGAMPEQIVVQALQCSHYSILWQLVKITDGS PSKEDLLVLRKTVKSFLAVCQQCLSNVNTPVKEQAFMLLCDLLMIFSHQLMTGGREGLQP LVFNPDTGLQSELLSFVMDHVFIDQDEENQSMEGDEEDEANKIEALHKRRNLLAAFSKLI IYDIVDMHAAADIFKHYMKYYNDYGDIIKETLSKTRQID
>6RRK_2 Double-strand-break repair protein rad21 homolog (chains C, D) PTKKLMMWKETGGVEKLFSLPAQPLWNNRLLKLFTRCLTP
STAG1 vulnerabilities for exploiting cohesin synthetic lethality in STAG2-deficient cancers. van der Lelij, P., Newman, J.A., Lieb, S. et al. Life Sci Alliance (2020) 3. DOI 10.26508/lsa.202000725 · PubMed
Other PDB entries of the same protein (UniProt Q8WVM7 (AlphaFold model), which also has an AlphaFold model), best resolution first:
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