Crystal structure of S. cerevisiae Get3 in the semi open conformation in complex with Get1 cytosolic domain at 4.5 angstrom resolution. Determined by X-ray diffraction at 4.5 Å resolution. Released 20 Jun 2012.
Explore 3VLC in 3D Show helices and sheets RCSB PDB PDBe
3VLC contains 20 α-helices and 10 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 |
|---|---|---|---|
| α-helix | 10-14 | 5 | |
| β-strand | 20-24 | 5 | 1 |
| α-helix | 31-44 | 14 | |
| β-strand | 51-55 | 5 | 1 |
| α-helix | 61-66 | 6 | |
| β-strand | 75-76 | 2 | 1 |
| β-strand | 78 | 1 | 2 |
| β-strand | 80 | 1 | 2 |
| β-strand | 83-87 | 5 | 1 |
| α-helix | 90-93 | 4 | |
| α-helix | 128-132 | 5 | |
| α-helix | 136-155 | 20 | |
| β-strand | 162-166 | 5 | 1 |
| α-helix | 176-178 | 3 | |
| α-helix | 179-184 | 6 | |
| α-helix | 219-230 | 12 | |
| β-strand | 236-243 | 8 | 1 |
| α-helix | 246-262 | 17 | |
| β-strand | 266-274 | 9 | 1 |
| α-helix | 277-279 | 3 | |
| α-helix | 290-305 | 16 | |
| β-strand | 310-315 | 6 | 1 |
| α-helix | 323-331 | 9 | |
| α-helix | 332-334 | 3 | |
| α-helix | 342-344 | 3 | |
| α-helix | 346-348 | 3 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| α-helix | 40-56 | 17 | |
| α-helix | 65-81 | 17 | |
| α-helix | 85-88 | 4 | |
| α-helix | 93-96 | 4 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| ATPase GET3 | A | protein | 354 | Saccharomyces cerevisiae | Q12154 (AlphaFold model) |
| Golgi to ER traffic protein 1 | E | protein | 94 | Saccharomyces cerevisiae | P53192 (AlphaFold model) |
>3VLC_1 ATPase GET3 (chains A) MDLTVEPNLHSLITSTTHKWIFVGGKGGVGKTTSSCSIAIQMALSQPNKQFLLISTDPAH NLSDAFGEKFGKDARKVTGMNNLSCMEIDPSAALKDMNDMAVSRANNNGSDGQGDDLGSL LQGGALADLTGSIPGIDEALSFMEVMKHIKRQEQDEGETFDTVIFDTAPTGHTLRFLQLP NTLSKLLEKFGEITNKLGPMLNSFMGAGNVDISGKLNELKANVETIRQQFTDPDLTTFVC VCISEFLSLYETERLIQELISYDMDVNSIIVNQLLFAENDQEHNCKRCQARWKMQKKYLD QIDELYEDFHVVKMPLCAGEIRGLNNLTKFSQFLNKEYNPITDGKVIYELEDKE
>3VLC_2 Golgi to ER traffic protein 1 (chains E) MGSSHHHHHHTNKYHEKWISKFAPGNELSKKYLAKVKERHELKEFNNSISAQDNYAKWTK NNRKLDSLDKEINNLKDEIQSENKAFQAHLHKLR
| ID | Name | Formula | Copies |
|---|---|---|---|
| ADP | Adenosine-5'-diphosphate | C10 H15 N5 O10 P2 | 1 |
Get1 stabilizes an open dimer conformation of get3 ATPase by binding two distinct interfaces. Kubota, K., Yamagata, A., Sato, Y. et al. J Mol Biol (2012) 422:366-375. DOI 10.1016/j.jmb.2012.05.045 · PubMed
Other PDB entries of the same protein (UniProt Q12154 (AlphaFold model), which also has an AlphaFold model), best resolution first:
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