Crystal structure of the N-terminal region of human cohesin subunit STAG1. Determined by X-ray diffraction at 2.02 Å resolution. Released 6 Feb 2019.
Explore 6QB5 in 3D Show helices and sheets RCSB PDB PDBe
6QB5 contains 92 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 | 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 | 199-211 | 13 | |
| 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 | 364-373 | 10 | |
| α-helix | 375-379 | 5 | |
| 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 | 136-141 | 6 | |
| α-helix | 144-152 | 9 | |
| α-helix | 163-165 | 3 | |
| α-helix | 169-171 | 3 | |
| α-helix | 174-189 | 16 | |
| α-helix | 193-195 | 3 | |
| α-helix | 199-211 | 13 | |
| α-helix | 216-255 | 40 | |
| α-helix | 258 | 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 | 329-337 | 9 | |
| α-helix | 338-340 | 3 | |
| α-helix | 344-358 | 15 | |
| α-helix | 361-363 | 3 | |
| α-helix | 364-373 | 10 | |
| α-helix | 375-380 | 6 | |
| 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 | 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 | 329-338 | 10 | |
| α-helix | 344-358 | 15 | |
| α-helix | 361-367 | 7 | |
| 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 | 144-152 | 9 | |
| α-helix | 169-171 | 3 | |
| α-helix | 174-189 | 16 | |
| α-helix | 193-195 | 3 | |
| α-helix | 199-211 | 13 | |
| α-helix | 216-250 | 35 | |
| 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 | 329-336 | 8 | |
| α-helix | 337-340 | 4 | |
| α-helix | 344-358 | 15 | |
| α-helix | 361-363 | 3 | |
| α-helix | 364-373 | 10 | |
| α-helix | 375-380 | 6 | |
| 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) |
>6QB5_1 Cohesin subunit SA-1 (chains A, B, C, D) SMGGTLFEVVKLGKSAMQSVVDDWIESYKQDRDIALLDLINFFIQCSGCRGTVRIEMFRN MQNAEIIRKMTEEFDEDSGDYPLTMPGPQWKKFRSNFCEFIGVLIRQCQYSIIYDEYMMD TVISLLTGLSDSQVRAFRHTSTLAAMKLMTALVNVALNLSIHQDNTQRQYEAERNKMIGK RANERLELLLQKRKELQENQDEIENMMNSIFKGIFVHRYRDAIAEIRAICIEEIGVWMKM YSDAFLNDSYLKYVGWTLHDRQGEVRLKCLKALQSLYTNRELFPKLELFTNRFKDRIVSM TLDKEYDVAVEAIRLVTLILHGSEEALSNEDCENVYHLV
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:
MolViewer shows 6QB5 directly in your browser with nothing to install. Switch between cartoon, ball-and-stick, spacefill and surface views, color by chain, secondary structure or B-factor, measure distances, angles and dihedrals, and share or embed the view.