PanDDA analysis group deposition -- Crystal Structure of human STAG1 in complex with Z2856434926. Determined by X-ray diffraction at 2.73 Å resolution. Released 21 Aug 2019.
Explore 5QSU in 3D Show helices and sheets RCSB PDB PDBe
5QSU contains 88 α-helices and 2 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 | 87-93 | 7 | |
| α-helix | 97-111 | 15 | |
| α-helix | 113-127 | 15 | |
| α-helix | 136-141 | 6 | |
| α-helix | 144-152 | 9 | |
| α-helix | 163-165 | 3 | |
| α-helix | 169-189 | 21 | |
| α-helix | 193-195 | 3 | |
| α-helix | 199-212 | 14 | |
| α-helix | 216-251 | 36 | |
| α-helix | 271-291 | 21 | |
| α-helix | 292-296 | 5 | |
| α-helix | 297-299 | 3 | |
| α-helix | 305-321 | 17 | |
| α-helix | 323-326 | 4 | |
| α-helix | 329-336 | 8 | |
| α-helix | 344-358 | 15 | |
| α-helix | 361-363 | 3 | |
| α-helix | 364-379 | 16 | |
| α-helix | 380-383 | 4 | |
| α-helix | 387-402 | 16 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| α-helix | 87-92 | 6 | |
| α-helix | 97-111 | 15 | |
| α-helix | 113-127 | 15 | |
| α-helix | 136-139 | 4 | |
| α-helix | 144-152 | 9 | |
| α-helix | 174-189 | 16 | |
| α-helix | 193-195 | 3 | |
| α-helix | 199-211 | 13 | |
| α-helix | 216-255 | 40 | |
| α-helix | 258 | 1 | |
| β-strand | 259 | 1 | 1 |
| β-strand | 262 | 1 | 1 |
| α-helix | 264-291 | 28 | |
| α-helix | 292-296 | 5 | |
| α-helix | 297-299 | 3 | |
| α-helix | 305-321 | 17 | |
| α-helix | 323-326 | 4 | |
| α-helix | 329-338 | 10 | |
| α-helix | 344-358 | 15 | |
| α-helix | 361-363 | 3 | |
| α-helix | 364-380 | 17 | |
| α-helix | 381-383 | 3 | |
| α-helix | 387-402 | 16 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| α-helix | 87-93 | 7 | |
| α-helix | 97-111 | 15 | |
| α-helix | 113-127 | 15 | |
| α-helix | 136-141 | 6 | |
| α-helix | 144-152 | 9 | |
| α-helix | 163-165 | 3 | |
| α-helix | 170-172 | 3 | |
| α-helix | 174-189 | 16 | |
| α-helix | 193-195 | 3 | |
| α-helix | 199-211 | 13 | |
| α-helix | 216-255 | 40 | |
| α-helix | 265-291 | 27 | |
| α-helix | 292-296 | 5 | |
| α-helix | 297-299 | 3 | |
| α-helix | 305-321 | 17 | |
| α-helix | 323-326 | 4 | |
| α-helix | 329-337 | 9 | |
| α-helix | 338-340 | 3 | |
| α-helix | 344-358 | 15 | |
| α-helix | 361-366 | 6 | |
| α-helix | 368-380 | 13 | |
| α-helix | 381-383 | 3 | |
| α-helix | 387-403 | 17 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| α-helix | 87-93 | 7 | |
| α-helix | 97-111 | 15 | |
| α-helix | 113-127 | 15 | |
| α-helix | 133-135 | 3 | |
| α-helix | 136-139 | 4 | |
| α-helix | 144-153 | 10 | |
| α-helix | 163-165 | 3 | |
| α-helix | 169-171 | 3 | |
| α-helix | 174-189 | 16 | |
| α-helix | 193-196 | 4 | |
| α-helix | 199-211 | 13 | |
| α-helix | 216-245 | 30 | |
| α-helix | 267-291 | 25 | |
| α-helix | 292-296 | 5 | |
| α-helix | 297-299 | 3 | |
| α-helix | 305-321 | 17 | |
| α-helix | 323-326 | 4 | |
| α-helix | 329-338 | 10 | |
| α-helix | 344-358 | 15 | |
| α-helix | 361-363 | 3 | |
| α-helix | 364-380 | 17 | |
| α-helix | 381-383 | 3 | |
| α-helix | 387-401 | 15 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| Cohesin subunit SA-1 | A, B, C, D | protein | 339 | Homo sapiens | Q8WVM7 (AlphaFold model) |
>5QSU_1 Cohesin subunit SA-1 (chains A, B, C, D) SMGGTLFEVVKLGKSAMQSVVDDWIESYKQDRDIALLDLINFFIQCSGCRGTVRIEMFRN MQNAEIIRKMTEEFDEDSGDYPLTMPGPQWKKFRSNFCEFIGVLIRQCQYSIIYDEYMMD TVISLLTGLSDSQVRAFRHTSTLAAMKLMTALVNVALNLSIHQDNTQRQYEAERNKMIGK RANERLELLLQKRKELQENQDEIENMMNSIFKGIFVHRYRDAIAEIRAICIEEIGVWMKM YSDAFLNDSYLKYVGWTLHDRQGEVRLKCLKALQSLYTNRELFPKLELFTNRFKDRIVSM TLDKEYDVAVEAIRLVTLILHGSEEALSNEDCENVYHLV
| ID | Name | Formula | Copies |
|---|---|---|---|
| O3D | 4-[(furan-2-yl)methyl]-1lambda~6~,4-thiazinane-1,1-dione | C9 H13 N O3 S | 1 |
PanDDA analysis group deposition. Newman, J.A., Katis, V.L., Gavard, A.E. et al. To be published.
Other PDB entries of the same protein (UniProt Q8WVM7 (AlphaFold model), which also has an AlphaFold model), best resolution first:
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