2WPV: S. cerevisiae Get4-Get5 complex
Crystal structure of S. cerevisiae Get4-Get5 complex. Determined by X-ray diffraction at 1.99 Å resolution. Released 26 Jan 2010.
- Method
- X-ray diffraction
- Resolution
- 1.99 Å
- Organism
- SACCHAROMYCES CEREVISIAE
- Chains
- 8
- Atoms
- 12,001
- Mol. weight
- 172.62 kDa
- Ligands
- HG
- Released
- 26 Jan 2010
Explore 2WPV in 3D
Show helices and sheets
RCSB PDB
PDBe
Secondary structure: helices and β-sheets
2WPV contains 74 α-helices and 16 β-strands across 8 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: 15 helices, 3 β-strands
| Element | Residues | Length | Sheet |
|---|
| α-helix | 13-26 | 14 | |
| α-helix | 29-45 | 17 | |
| α-helix | 49-65 | 17 | |
| α-helix | 69-85 | 17 | |
| α-helix | 92-102 | 11 | |
| 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 | |
Chains B, F and H: 3 helices, 1 β-strand
| Element | Residues | Length | Sheet |
|---|
| α-helix | 8-20 | 13 | |
| 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 | 12-26 | 15 | |
| 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 | 162-176 | 15 | |
| 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: 4 helices, 1 β-strand
| Element | Residues | Length | Sheet |
|---|
| α-helix | 8-21 | 14 | |
| β-strand | 32 | 1 | 3 |
| α-helix | 35-37 | 3 | |
| α-helix | 44-48 | 5 | |
| α-helix | 51-53 | 3 | |
Chain E: 16 helices, 3 β-strands
| Element | Residues | Length | Sheet |
|---|
| α-helix | 14-26 | 13 | |
| α-helix | 29-45 | 17 | |
| α-helix | 49-65 | 17 | |
| α-helix | 69-85 | 17 | |
| α-helix | 88-90 | 3 | |
| α-helix | 92-103 | 12 | |
| 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 | |
Chain G: 15 helices, 3 β-strands
| Element | Residues | Length | Sheet |
|---|
| α-helix | 13-25 | 13 | |
| 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 | 7 |
| α-helix | 204-222 | 19 | |
| β-strand | 226-231 | 6 | 8 |
| β-strand | 234-239 | 6 | 8 |
| α-helix | 243-257 | 15 | |
| α-helix | 260-269 | 10 | |
| α-helix | 271-276 | 6 | |
| α-helix | 278-289 | 12 | |
Molecules and chains
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|
| UPF0363 protein YOR164C | A, C, E, G | protein | 312 | SACCHAROMYCES CEREVISIAE | Q12125 (AlphaFold model) |
| Ubiquitin-like protein MDY2 | B, D, F, H | protein | 59 | SACCHAROMYCES CEREVISIAE | Q12285 (AlphaFold model) |
Sequence of entity 1 (A, C, E, G), FASTA
>2WPV_1 UPF0363 PROTEIN YOR164C (chains A, C, E, G)
MVPAESNAVQAKLAKTLQRFENKIKAGDYYEAHQTLRTIANRYVRSKSYEHAIELISQGA
LSFLKAKQGGSGTDLIFYLLEVYDLAEVKVDDISVARLVRLIAELDPSEPNLKDVITGMN
NWSIKFSEYKFGDPYLHNTIGSKLLEGDFVYEAERYFMLGTHDSMIKYVDLLWDWLCQVD
DIEDSTVAEFFSRLVFNYLFISNISFAHESKDIFLERFIEKFHPKYEKIDKNGYEIVFFE
DYSDLNFLQLLLITCQTKDKSYFLNLKNHYLDFSQAYKSELEFLGQEYFNIVAPKQTNFL
QDMMSGFLGGSK
Sequence of entity 2 (B, D, F, H), FASTA
>2WPV_2 UBIQUITIN-LIKE PROTEIN MDY2 (chains B, D, F, H)
MSTSASGPEHEFVSKFLTLATLTEPKLPKSYTKPLKDVTNLGVPLPTLKYKYKQNRAKK
Ligands and cofactors
| ID | Name | Formula | Copies |
|---|
| HG | Mercury (II) ion | Hg | 4 |
Primary citation
Crystal Structure of Get4-Get5 Complex and its Interactions with Sgt2, Get3, and Ydj1. Chang, Y.-W., Chuang, Y.-C., Ho, Y.-C. et al. J Biol Chem (2010) 285:9962. DOI 10.1074/JBC.M109.087098 · PubMed
Other PDB entries of the same protein (UniProt Q12125 (AlphaFold model), which also has an AlphaFold model), best resolution first:
- 3LKU 2.8 Å, Crystal structure of S. cerevisiae Get4 in complex with an N-terminal fragment of Get5
- 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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