3SJA: S. cerevisiae Get3 in the open state
Crystal structure of S. cerevisiae Get3 in the open state in complex with Get1 cytosolic domain. Determined by X-ray diffraction at 3.0 Å resolution. Released 6 Jul 2011.
- Method
- X-ray diffraction
- Resolution
- 3.0 Å
- Organism
- Saccharomyces cerevisiae
- Chains
- 10
- Atoms
- 15,873
- Mol. weight
- 242.67 kDa
- Ligands
- ZN, PO4
- Released
- 6 Jul 2011
Explore 3SJA in 3D
Show helices and sheets
RCSB PDB
PDBe
Secondary structure: helices and β-sheets
3SJA contains 87 α-helices and 40 β-strands across 10 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.
Chain A: 17 helices, 8 β-strands
| Element | Residues | Length | Sheet |
|---|
| α-helix | 10-14 | 5 | |
| β-strand | 20-24 | 5 | 1 |
| α-helix | 31-45 | 15 | |
| β-strand | 51-55 | 5 | 1 |
| α-helix | 62-66 | 5 | |
| β-strand | 76 | 1 | 1 |
| β-strand | 83-87 | 5 | 1 |
| α-helix | 90-103 | 14 | |
| α-helix | 118-130 | 13 | |
| α-helix | 136-156 | 21 | |
| β-strand | 162-166 | 5 | 1 |
| α-helix | 175-178 | 4 | |
| α-helix | 179-194 | 16 | |
| α-helix | 199-204 | 6 | |
| α-helix | 206-230 | 25 | |
| β-strand | 236-243 | 8 | 1 |
| α-helix | 246-260 | 15 | |
| β-strand | 265-274 | 10 | 1 |
| α-helix | 277-279 | 3 | |
| α-helix | 286-303 | 18 | |
| β-strand | 310-315 | 6 | 1 |
| α-helix | 316 | 1 | |
| α-helix | 324-331 | 8 | |
| α-helix | 332-334 | 3 | |
| α-helix | 340-353 | 14 | |
Chain B: 15 helices, 8 β-strands
| Element | Residues | Length | Sheet |
|---|
| α-helix | 10-14 | 5 | |
| β-strand | 20-24 | 5 | 2 |
| α-helix | 31-45 | 15 | |
| β-strand | 51-55 | 5 | 2 |
| α-helix | 62-66 | 5 | |
| β-strand | 75-76 | 2 | 2 |
| β-strand | 83-87 | 5 | 2 |
| α-helix | 90-103 | 14 | |
| α-helix | 117-130 | 14 | |
| α-helix | 136-156 | 21 | |
| β-strand | 162-166 | 5 | 2 |
| α-helix | 179-194 | 16 | |
| α-helix | 201-204 | 4 | |
| α-helix | 206-230 | 25 | |
| β-strand | 236-243 | 8 | 2 |
| α-helix | 246-261 | 16 | |
| β-strand | 266-274 | 9 | 2 |
| α-helix | 286-305 | 20 | |
| β-strand | 310-315 | 6 | 2 |
| α-helix | 316 | 1 | |
| α-helix | 324-331 | 8 | |
| α-helix | 332-334 | 3 | |
| α-helix | 344-353 | 10 | |
Chains C, D, H and J: 2 helices, 0 β-strands
| Element | Residues | Length | Sheet |
|---|
| α-helix | 37-56 | 20 | |
| α-helix | 65-91 | 27 | |
Chain E: 15 helices, 8 β-strands
| Element | Residues | Length | Sheet |
|---|
| α-helix | 10-14 | 5 | |
| β-strand | 20-24 | 5 | 3 |
| α-helix | 31-45 | 15 | |
| β-strand | 51-55 | 5 | 3 |
| α-helix | 62-66 | 5 | |
| β-strand | 75-76 | 2 | 3 |
| β-strand | 83-87 | 5 | 3 |
| α-helix | 90-103 | 14 | |
| α-helix | 118-130 | 13 | |
| α-helix | 136-156 | 21 | |
| β-strand | 162-166 | 5 | 3 |
| α-helix | 179-194 | 16 | |
| α-helix | 199-204 | 6 | |
| α-helix | 206-230 | 25 | |
| β-strand | 236-243 | 8 | 3 |
| α-helix | 246-261 | 16 | |
| β-strand | 266-274 | 9 | 3 |
| α-helix | 286-305 | 20 | |
| β-strand | 310-315 | 6 | 3 |
| α-helix | 316 | 1 | |
| α-helix | 324-331 | 8 | |
| α-helix | 332-334 | 3 | |
| α-helix | 344-352 | 9 | |
Chain F: 15 helices, 8 β-strands
| Element | Residues | Length | Sheet |
|---|
| α-helix | 10-13 | 4 | |
| β-strand | 20-24 | 5 | 4 |
| α-helix | 31-45 | 15 | |
| β-strand | 51-55 | 5 | 4 |
| α-helix | 62-66 | 5 | |
| β-strand | 75-76 | 2 | 4 |
| β-strand | 83-87 | 5 | 4 |
| α-helix | 90-104 | 15 | |
| α-helix | 117-130 | 14 | |
| α-helix | 136-156 | 21 | |
| β-strand | 162-166 | 5 | 4 |
| α-helix | 173-178 | 6 | |
| α-helix | 179-194 | 16 | |
| α-helix | 199-204 | 6 | |
| α-helix | 206-230 | 25 | |
| β-strand | 236-243 | 8 | 4 |
| α-helix | 246-261 | 16 | |
| β-strand | 266-274 | 9 | 4 |
| α-helix | 277-279 | 3 | |
| α-helix | 286-305 | 20 | |
| β-strand | 310-315 | 6 | 4 |
| α-helix | 324-335 | 12 | |
| α-helix | 344-353 | 10 | |
Chain G: 2 helices, 0 β-strands
| Element | Residues | Length | Sheet |
|---|
| α-helix | 37-57 | 21 | |
| α-helix | 65-91 | 27 | |
Chain I: 15 helices, 8 β-strands
| Element | Residues | Length | Sheet |
|---|
| α-helix | 10-13 | 4 | |
| β-strand | 20-24 | 5 | 5 |
| α-helix | 31-45 | 15 | |
| β-strand | 51-55 | 5 | 5 |
| α-helix | 62-66 | 5 | |
| β-strand | 75-76 | 2 | 5 |
| β-strand | 83-87 | 5 | 5 |
| α-helix | 90-104 | 15 | |
| α-helix | 117-130 | 14 | |
| α-helix | 136-156 | 21 | |
| β-strand | 162-166 | 5 | 5 |
| α-helix | 173-178 | 6 | |
| α-helix | 179-194 | 16 | |
| α-helix | 199-204 | 6 | |
| α-helix | 206-230 | 25 | |
| β-strand | 236-243 | 8 | 5 |
| α-helix | 246-261 | 16 | |
| β-strand | 266-274 | 9 | 5 |
| α-helix | 277-279 | 3 | |
| α-helix | 286-305 | 20 | |
| β-strand | 310-315 | 6 | 5 |
| α-helix | 324-335 | 12 | |
| α-helix | 344-352 | 9 | |
Molecules and chains
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|
| ATPase GET3 | A, B, E, F, I | protein | 362 | Saccharomyces cerevisiae | Q12154 (AlphaFold model) |
| Golgi to ER traffic protein 1 | C, D, G, H, J | protein | 65 | Saccharomyces cerevisiae | P53192 (AlphaFold model) |
Sequence of entity 1 (A, B, E, F, I), FASTA
>3SJA_1 ATPase GET3 (chains A, B, E, F, I)
MDLTVEPNLHSLITSTTHKWIFVGGKGGVGKTTSSCSIAIQMALSQPNKQFLLISTDPAH
NLSDAFGEKFGKDARKVTGMNNLSCMEIDPSAALKDMNDMAVSRANNNGSDGQGDDLGSL
LQGGALADLTGSIPGIDEALSFMEVMKHIKRQEQGEGETFDTVIFDTAPTGHTLRFLQLP
NTLSKLLEKFGEITNKLGPMLNSFMGAGNVDISGKLNELKANVETIRQQFTDPDLTTFVC
VCISEFLSLYETERLIQELISYDMDVNSIIVNQLLFAENDQEHNCKRCQARWKMQKKYLD
QIDELYEDFHVVKMPLCAGEIRGLNNLTKFSQFLNKEYNPITDGKVIYELEDKELEHHHH
HH
Sequence of entity 2 (C, D, G, H, J), FASTA
>3SJA_2 Golgi to ER traffic protein 1 (chains C, D, G, H, J)
MNELSKKYLAKVKERHELKEFNNSISAQDNYAKWTKNNRKLDSLDKEINNLKDEIQSENH
HHHHH
Ligands and cofactors
| ID | Name | Formula | Copies |
|---|
| ZN | Zinc ion | Zn | 3 |
| PO4 | Phosphate ion | O4 P | 7 |
Primary citation
Structural basis for tail-anchored membrane protein biogenesis by the Get3-receptor complex. Stefer, S., Reitz, S., Wang, F. et al. Science (2011) 333:758-762. DOI 10.1126/science.1207125 · PubMed
Other PDB entries of the same protein (UniProt Q12154 (AlphaFold model), which also has an AlphaFold model), best resolution first:
- 2WOJ 1.99 Å, ADP-AlF4 complex of S. cerevisiae GET3
- 4XTR 2.05 Å, Structure of Get3 bound to the transmembrane domain of Pep12
- 3ZS9 2.1 Å, S. cerevisiae Get3-ADP-AlF4- complex with a cytosolic Get2 fragment
- 3H84 2.3 Å, Crystal structure of GET3
- 4XVU 2.35 Å, Structure of Get3 bound to the transmembrane domain of Nyv1
- 4XWO 2.75 Å, Structure of Get3 bound to the transmembrane domain of Sec22
- 3A36 2.8 Å, Structural insight into the membrane insertion of tail-anchored proteins by Get3
- 5BW8 2.8 Å, 2.8 A crystal structure of a Get3-Get4-Get5 intermediate complex from S.cerevisiae
- 3A37 3.0 Å, Structural insight into the membrane insertion of tail-anchored proteins by Get3
- 3B2E 3.0 Å, Crystal structure of S. cerevisiae Get3 in the open conformation in complex with Get1…
- 3ZS8 3.0 Å, S. cerevisiae Get3 complexed with a cytosolic Get1 fragment
- 9NS5 3.19 Å, Get3(D57N)-Get4/5 Complex (ATP-bound)
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