PanDDA analysis group deposition -- Crystal Structure of human STAG1 in complex with Z2856434783. Determined by X-ray diffraction at 2.76 Å resolution. Released 21 Aug 2019.
Explore 5QSV in 3D Show helices and sheets RCSB PDB PDBe
5QSV contains 83 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 | 172-188 | 17 | |
| α-helix | 189-191 | 3 | |
| α-helix | 199-210 | 12 | |
| α-helix | 216-244 | 29 | |
| α-helix | 246-249 | 4 | |
| α-helix | 268-291 | 24 | |
| 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 | 364-380 | 17 | |
| α-helix | 381-383 | 3 | |
| α-helix | 389-401 | 13 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| α-helix | 87-93 | 7 | |
| α-helix | 97-111 | 15 | |
| α-helix | 113-128 | 16 | |
| α-helix | 137-140 | 4 | |
| α-helix | 144-152 | 9 | |
| α-helix | 163-165 | 3 | |
| α-helix | 169-171 | 3 | |
| α-helix | 174-189 | 16 | |
| α-helix | 199-210 | 12 | |
| α-helix | 216-250 | 35 | |
| α-helix | 269-291 | 23 | |
| 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 | 364-380 | 17 | |
| α-helix | 381-383 | 3 | |
| α-helix | 387-401 | 15 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| α-helix | 87-91 | 5 | |
| α-helix | 97-111 | 15 | |
| α-helix | 113-127 | 15 | |
| α-helix | 136-141 | 6 | |
| α-helix | 144-153 | 10 | |
| α-helix | 169-172 | 4 | |
| α-helix | 174-189 | 16 | |
| α-helix | 193-195 | 3 | |
| α-helix | 199-211 | 13 | |
| α-helix | 216-258 | 43 | |
| α-helix | 266-291 | 26 | |
| 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 | 344-359 | 16 | |
| α-helix | 364-367 | 4 | |
| α-helix | 368-380 | 13 | |
| 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 | 136-140 | 5 | |
| α-helix | 144-151 | 8 | |
| α-helix | 170-189 | 20 | |
| α-helix | 193-195 | 3 | |
| α-helix | 199-211 | 13 | |
| α-helix | 216-244 | 29 | |
| α-helix | 246-252 | 7 | |
| 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 | 389-402 | 14 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| Cohesin subunit SA-1 | A, B, C, D | protein | 339 | Homo sapiens | Q8WVM7 (AlphaFold model) |
>5QSV_1 Cohesin subunit SA-1 (chains A, B, C, D) SMGGTLFEVVKLGKSAMQSVVDDWIESYKQDRDIALLDLINFFIQCSGCRGTVRIEMFRN MQNAEIIRKMTEEFDEDSGDYPLTMPGPQWKKFRSNFCEFIGVLIRQCQYSIIYDEYMMD TVISLLTGLSDSQVRAFRHTSTLAAMKLMTALVNVALNLSIHQDNTQRQYEAERNKMIGK RANERLELLLQKRKELQENQDEIENMMNSIFKGIFVHRYRDAIAEIRAICIEEIGVWMKM YSDAFLNDSYLKYVGWTLHDRQGEVRLKCLKALQSLYTNRELFPKLELFTNRFKDRIVSM TLDKEYDVAVEAIRLVTLILHGSEEALSNEDCENVYHLV
| ID | Name | Formula | Copies |
|---|---|---|---|
| O3G | N-benzyl-1-(4-fluorophenyl)methanamine | C14 H14 F N | 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:
MolViewer shows 5QSV 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.