2G3K: C-terminal domain of Vps28
Crystal structure of the C-terminal domain of Vps28. Determined by X-ray diffraction at 3.05 Å resolution. Released 27 Jun 2006.
- Method
- X-ray diffraction
- Resolution
- 3.05 Å
- Organism
- Saccharomyces cerevisiae
- Chains
- 7
- Atoms
- 5,446
- Mol. weight
- 76.67 kDa
- Released
- 27 Jun 2006
Explore 2G3K in 3D
Show helices and sheets
RCSB PDB
PDBe
Secondary structure: helices and β-sheets
2G3K contains 30 α-helices and 12 β-strands across 7 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: 5 helices, 2 β-strands
| Element | Residues | Length | Sheet |
|---|
| α-helix | 150-167 | 18 | |
| β-strand | 173 | 1 | 1 |
| α-helix | 174-191 | 18 | |
| α-helix | 199-210 | 12 | |
| α-helix | 212-213 | 2 | |
| β-strand | 217 | 1 | 1 |
| α-helix | 220-240 | 21 | |
Chain B: 4 helices, 2 β-strands
| Element | Residues | Length | Sheet |
|---|
| α-helix | 150-168 | 19 | |
| β-strand | 173 | 1 | 2 |
| α-helix | 174-189 | 16 | |
| α-helix | 199-210 | 12 | |
| β-strand | 217 | 1 | 2 |
| α-helix | 220-238 | 19 | |
Chains C and F: 4 helices, 2 β-strands
| Element | Residues | Length | Sheet |
|---|
| α-helix | 150-168 | 19 | |
| β-strand | 173 | 1 | 3 |
| α-helix | 174-191 | 18 | |
| α-helix | 199-210 | 12 | |
| β-strand | 217 | 1 | 3 |
| α-helix | 220-239 | 20 | |
Chain D: 4 helices, 0 β-strands
| Element | Residues | Length | Sheet |
|---|
| α-helix | 150-168 | 19 | |
| α-helix | 174-191 | 18 | |
| α-helix | 199-211 | 13 | |
| α-helix | 220-239 | 20 | |
Chain E: 5 helices, 2 β-strands
| Element | Residues | Length | Sheet |
|---|
| α-helix | 150-168 | 19 | |
| β-strand | 173 | 1 | 4 |
| α-helix | 174-189 | 16 | |
| α-helix | 199-210 | 12 | |
| α-helix | 213 | 1 | |
| β-strand | 217 | 1 | 4 |
| α-helix | 220-239 | 20 | |
Chain G: 4 helices, 2 β-strands
| Element | Residues | Length | Sheet |
|---|
| α-helix | 150-167 | 18 | |
| β-strand | 173 | 1 | 6 |
| α-helix | 174-191 | 18 | |
| α-helix | 199-210 | 12 | |
| β-strand | 217 | 1 | 6 |
| α-helix | 220-239 | 20 | |
Molecules and chains
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|
| Vacuolar protein sorting-associated protein VPS28 | A, B, C, D, E, F, G | protein | 94 | Saccharomyces cerevisiae | Q02767 (AlphaFold model) |
Sequence of entity 1 (A, B, C, D, E, F, G), FASTA
>2G3K_1 Vacuolar protein sorting-associated protein VPS28 (chains A, B, C, D, E, F, G)
FNAKYVAEATGNFITVMDALKLNYNAKDQLHPLLAELLISINRVTRDDFENRSKLIDWIV
RINKLSIGDTLTETQIRELLFDLELAYKSFYALL
Primary citation
The crystal structure of the C-terminal domain of Vps28 reveals a conserved surface required for Vps20 recruitment. Pineda-Molina, E., Belrhali, H., Piefer, A.J. et al. Traffic (2006) 7:1007-1016. DOI 10.1111/j.1600-0854.2006.00440.x · PubMed
Other PDB entries of the same protein (UniProt Q02767 (AlphaFold model), which also has an AlphaFold model), best resolution first:
- 2J9U 2.0 Å, 2 Angstrom X-ray structure of the yeast ESCRT-I Vps28 C-terminus in complex with the…
- 2J9V 2.0 Å, 2 Angstrom X-ray structure of the yeast ESCRT-I Vps28 C-terminus
- 2F6M 2.1 Å, Structure of a Vps23-C:Vps28-N subcomplex
- 2P22 2.7 Å, Structure of the Yeast ESCRT-I Heterotetramer Core
- 2F66 2.8 Å, Structure of the ESCRT-I endosomal trafficking complex
- 2CAZ 3.6 Å, ESCRT-I core
Browse structure collections
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