Crystal structure of ATPase domain of Ssb1 chaperone, a member of the HSP70 family, from Saccharomyces cerevisiae. Determined by X-ray diffraction at 1.92 Å resolution. Released 24 Mar 2009.
Explore 3GL1 in 3D Show helices and sheets RCSB PDB PDBe
3GL1 contains 37 α-helices and 43 β-strands across 2 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 | 5 | 1 | 1 |
| β-strand | 10-13 | 4 | 2 |
| β-strand | 18-19 | 2 | 3 |
| β-strand | 20-24 | 5 | 2 |
| β-strand | 28-30 | 3 | 2 |
| α-helix | 31-32 | 2 | |
| β-strand | 40-41 | 2 | 3 |
| β-strand | 44-46 | 3 | 4 |
| β-strand | 51-53 | 3 | 4 |
| α-helix | 55-59 | 5 | |
| α-helix | 61-63 | 3 | |
| α-helix | 65-67 | 3 | |
| β-strand | 68-69 | 2 | 4 |
| α-helix | 72-74 | 3 | |
| α-helix | 83-89 | 7 | |
| β-strand | 95-99 | 5 | 5 |
| β-strand | 102-109 | 8 | 5 |
| β-strand | 112-116 | 5 | 5 |
| α-helix | 118-137 | 20 | |
| β-strand | 140 | 1 | 1 |
| β-strand | 143-148 | 6 | 2 |
| α-helix | 154-166 | 13 | |
| β-strand | 170-176 | 7 | 2 |
| α-helix | 177-184 | 8 | |
| β-strand | 196-203 | 8 | 6 |
| β-strand | 208-216 | 9 | 6 |
| β-strand | 219-228 | 10 | 6 |
| α-helix | 233-252 | 20 | |
| α-helix | 260-276 | 17 | |
| β-strand | 282-291 | 10 | 7 |
| β-strand | 294-301 | 8 | 7 |
| α-helix | 302-308 | 7 | |
| α-helix | 310-315 | 6 | |
| α-helix | 317-327 | 11 | |
| α-helix | 331-333 | 3 | |
| β-strand | 336-340 | 5 | 6 |
| α-helix | 342-345 | 4 | |
| α-helix | 347-356 | 10 | |
| α-helix | 360-362 | 3 | |
| β-strand | 363 | 1 | 6 |
| α-helix | 371-383 | 13 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| β-strand | 5 | 1 | 8 |
| β-strand | 9-14 | 6 | 9 |
| β-strand | 18-24 | 7 | 9 |
| β-strand | 28-30 | 3 | 9 |
| β-strand | 40-41 | 2 | 9 |
| β-strand | 44-46 | 3 | 10 |
| β-strand | 51-53 | 3 | 10 |
| α-helix | 55-58 | 4 | |
| α-helix | 65-67 | 3 | |
| β-strand | 68-69 | 2 | 10 |
| α-helix | 72-74 | 3 | |
| α-helix | 83-89 | 7 | |
| β-strand | 95-99 | 5 | 11 |
| β-strand | 102-109 | 8 | 11 |
| β-strand | 112-116 | 5 | 11 |
| α-helix | 118-137 | 20 | |
| β-strand | 140 | 1 | 8 |
| β-strand | 143-148 | 6 | 9 |
| α-helix | 154-166 | 13 | |
| β-strand | 170-176 | 7 | 9 |
| α-helix | 177-184 | 8 | |
| α-helix | 189-191 | 3 | |
| β-strand | 196-203 | 8 | 12 |
| β-strand | 208-216 | 9 | 12 |
| β-strand | 219-228 | 10 | 12 |
| α-helix | 233-252 | 20 | |
| α-helix | 260-277 | 18 | |
| β-strand | 282-291 | 10 | 13 |
| β-strand | 294-301 | 8 | 13 |
| α-helix | 302-308 | 7 | |
| α-helix | 310-315 | 6 | |
| α-helix | 317-327 | 11 | |
| α-helix | 331-333 | 3 | |
| β-strand | 336-340 | 5 | 12 |
| α-helix | 342-345 | 4 | |
| α-helix | 347-356 | 10 | |
| α-helix | 360-362 | 3 | |
| β-strand | 363 | 1 | 12 |
| α-helix | 371-382 | 12 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| Heat shock protein SSB1 | A, B | protein | 387 | Saccharomyces cerevisiae | P11484 (AlphaFold model) |
>3GL1_1 Heat shock protein SSB1 (chains A, B) SNAMAEGVFQGAIGIDLGTTYSCVATYESSVEIIANEQGNRVTPSFVAFTPEERLIGDAA KNQAALNPRNTVFDAKRLIGRRFDDESVQKDMKTWPFKVIDVDGNPVIEVQYLEETKTFS PQEISAMVLTKMKEIAEAKIGKKVEKAVITVPAYFNDAQRQATKDAGAISGLNVLRIINE PTAAAIAYGLGAGKSEKERHVLIFDLGGGTFDVSLLHIAGGVYTVKSTSGNTHLGGQDFD TNLLEHFKAEFKKKTGLDISDDARALRRLRTAAERAKRTLSSVTQTTVEVDSLFDGEDFE SSLTRARFEDLNAALFKSTLEPVEQVLKDAKISKSQIDEVVLVGGSTRIPKVQKLLSDFF DGKQLEKSINPDEAVAYGAAVQGAILT
| ID | Name | Formula | Copies |
|---|---|---|---|
| MG | Magnesium ion | Mg | 3 |
Water and common crystallization additives (GOL, CL) are not listed.
Crystal structure of ATPase domain of Ssb1 chaperone, member of the HSP70 family from Saccharomyces cerevisiae. Osipiuk, J., Li, H., Bargassa, M. et al. To be published.
Other PDB entries of the same protein (UniProt P11484 (AlphaFold model), which also has an AlphaFold model), best resolution first:
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