3LKU: S. cerevisiae Get4
Crystal structure of S. cerevisiae Get4 in complex with an N-terminal fragment of Get5. Determined by X-ray diffraction at 2.8 Å resolution. Released 23 Jun 2010.
- Method
- X-ray diffraction
- Resolution
- 2.8 Å
- Organism
- Saccharomyces cerevisiae
- Chains
- 6
- Atoms
- 8,539
- Mol. weight
- 121.78 kDa
- Ligands
- PRO
- Released
- 23 Jun 2010
Explore 3LKU in 3D
Show helices and sheets
RCSB PDB
PDBe
Secondary structure: helices and β-sheets
3LKU contains 58 α-helices and 12 β-strands across 6 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: 16 helices, 3 β-strands
| Element | Residues | Length | Sheet |
|---|
| α-helix | 15-25 | 11 | |
| α-helix | 29-45 | 17 | |
| α-helix | 49-65 | 17 | |
| α-helix | 69-85 | 17 | |
| α-helix | 92-104 | 13 | |
| α-helix | 112-125 | 14 | |
| α-helix | 134-146 | 13 | |
| α-helix | 150-158 | 9 | |
| α-helix | 162-178 | 17 | |
| α-helix | 184-200 | 17 | |
| β-strand | 203 | 1 | 1 |
| α-helix | 204-222 | 19 | |
| β-strand | 226-231 | 6 | 2 |
| β-strand | 234-239 | 6 | 2 |
| α-helix | 243-257 | 15 | |
| α-helix | 260-269 | 10 | |
| α-helix | 271-276 | 6 | |
| α-helix | 278-289 | 12 | |
| α-helix | 294-297 | 4 | |
Chain B: 4 helices, 1 β-strand
| Element | Residues | Length | Sheet |
|---|
| α-helix | 4-6 | 3 | |
| α-helix | 7-20 | 14 | |
| β-strand | 32 | 1 | 1 |
| α-helix | 35-37 | 3 | |
| α-helix | 44-48 | 5 | |
Chain C: 15 helices, 3 β-strands
| Element | Residues | Length | Sheet |
|---|
| α-helix | 10-25 | 16 | |
| α-helix | 29-45 | 17 | |
| α-helix | 49-65 | 17 | |
| α-helix | 69-85 | 17 | |
| α-helix | 92-104 | 13 | |
| α-helix | 112-125 | 14 | |
| α-helix | 134-146 | 13 | |
| α-helix | 150-158 | 9 | |
| α-helix | 162-178 | 17 | |
| α-helix | 184-200 | 17 | |
| β-strand | 203 | 1 | 3 |
| α-helix | 204-222 | 19 | |
| β-strand | 226-231 | 6 | 4 |
| β-strand | 234-239 | 6 | 4 |
| α-helix | 243-257 | 15 | |
| α-helix | 260-269 | 10 | |
| α-helix | 271-276 | 6 | |
| α-helix | 278-289 | 12 | |
Chain D: 3 helices, 1 β-strand
| Element | Residues | Length | Sheet |
|---|
| α-helix | 7-20 | 14 | |
| β-strand | 32 | 1 | 3 |
| α-helix | 35-37 | 3 | |
| α-helix | 44-48 | 5 | |
Chain E: 16 helices, 3 β-strands
| Element | Residues | Length | Sheet |
|---|
| α-helix | 10-25 | 16 | |
| α-helix | 29-45 | 17 | |
| α-helix | 49-65 | 17 | |
| α-helix | 69-85 | 17 | |
| α-helix | 92-104 | 13 | |
| α-helix | 112-125 | 14 | |
| α-helix | 134-146 | 13 | |
| α-helix | 150-158 | 9 | |
| α-helix | 162-178 | 17 | |
| α-helix | 184-200 | 17 | |
| β-strand | 203 | 1 | 5 |
| α-helix | 204-222 | 19 | |
| β-strand | 226-231 | 6 | 6 |
| β-strand | 234-239 | 6 | 6 |
| α-helix | 243-257 | 15 | |
| α-helix | 260-269 | 10 | |
| α-helix | 271-276 | 6 | |
| α-helix | 278-289 | 12 | |
| α-helix | 294-297 | 4 | |
Chain F: 4 helices, 1 β-strand
| Element | Residues | Length | Sheet |
|---|
| α-helix | 4-6 | 3 | |
| α-helix | 7-21 | 15 | |
| β-strand | 32 | 1 | 5 |
| α-helix | 35-37 | 3 | |
| α-helix | 44-48 | 5 | |
Molecules and chains
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|
| UPF0363 protein YOR164C | A, C, E | protein | 292 | Saccharomyces cerevisiae | Q12125 (AlphaFold model) |
| Ubiquitin-like protein MDY2 | B, D, F | protein | 54 | Saccharomyces cerevisiae | Q12285 (AlphaFold model) |
Sequence of entity 1 (A, C, E), FASTA
>3LKU_1 UPF0363 protein YOR164C (chains A, C, E)
MGAKLAKTLQRFENKIKAGDYYEAHQTLRTIANRYVRSKSYEHAIELISQGALSFLKAKQ
GGSGTDLIFYLLEVYDLAEVKVDDISVARLVRLIAELDPSEPNLKDVITGMNNWSIKFSE
YKFGDPYLHNTIGSKLLEGDFVYEAERYFMLGTHDSMIKYVDLLWDWLCQVDDIEDSTVA
EFFSRLVFNYLFISNISFAHESKDIFLERFIEKFHPKYEKIDKNGYEIVFFEDYSDLNFL
QLLLITCQTKDKSYFLNLKNHYLDFSQAYKSELEFLGQEYFNIVAPKQTNFL
Sequence of entity 2 (B, D, F), FASTA
>3LKU_2 Ubiquitin-like protein MDY2 (chains B, D, F)
TSASGPEHEFVSKFLTLATLTEPKLPKSYTKPLKDVTNLGVPLPTLKYKYKQNR
Ligands and cofactors
| ID | Name | Formula | Copies |
|---|
| PRO | Proline | C5 H9 N O2 | 2 |
Primary citation
Structural characterization of the Get4/Get5 complex and its interaction with Get3. Chartron, J.W., Suloway, C.J., Zaslaver, M. et al. Proc Natl Acad Sci U S A (2010) 107:12127-12132. DOI 10.1073/pnas.1006036107 · PubMed
Other PDB entries of the same protein (UniProt Q12125 (AlphaFold model), which also has an AlphaFold model), best resolution first:
- 2WPV 1.99 Å, Crystal structure of S. cerevisiae Get4-Get5 complex
- 5BW8 2.8 Å, 2.8 A crystal structure of a Get3-Get4-Get5 intermediate complex from S.cerevisiae
- 9NS5 3.19 Å, Get3(D57N)-Get4/5 Complex (ATP-bound)
- 4PWX 5.4 Å, Crystal structure of an ATP-bound Get3-Get4-Get5 complex from S.cerevisiae
- 5BWK 6.0 Å, 6.0 A Crystal structure of a Get3-Get4-Get5 intermediate complex from S.cerevisiae
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