Structure of the Yeast ESCRT-I Heterotetramer Core. Determined by X-ray diffraction at 2.7 Å resolution. Released 5 Jun 2007.
Explore 2P22 in 3D Show helices and sheets RCSB PDB PDBe
2P22 contains 25 α-helices and 3 β-strands across 4 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 | 219-246 | 28 | |
| α-helix | 248-251 | 4 | |
| α-helix | 254-289 | 36 | |
| α-helix | 291-303 | 13 | |
| α-helix | 314-316 | 3 | |
| β-strand | 318-319 | 2 | 1 |
| α-helix | 323-351 | 29 | |
| α-helix | 356-381 | 26 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| α-helix | 14-18 | 5 | |
| α-helix | 31-57 | 27 | |
| α-helix | 64-83 | 20 | |
| α-helix | 111-115 | 5 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| α-helix | 23-33 | 11 | |
| α-helix | 48-52 | 5 | |
| α-helix | 55-57 | 3 | |
| α-helix | 62-70 | 9 | |
| α-helix | 72-78 | 7 | |
| α-helix | 79-82 | 4 | |
| α-helix | 86-143 | 58 | |
| α-helix | 147-170 | 24 | |
| α-helix | 178-205 | 28 | |
| β-strand | 211 | 1 | 1 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| α-helix | 4-11 | 8 | |
| β-strand | 15-16 | 2 | 1 |
| α-helix | 31-34 | 4 | |
| α-helix | 37-39 | 3 | |
| α-helix | 41-65 | 25 | |
| α-helix | 67-78 | 12 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| Suppressor protein STP22 of temperature-sensitive alpha-factor receptor and arginine permease | A | protein | 174 | Saccharomyces cerevisiae | P25604 (AlphaFold model) |
| Vacuolar protein sorting-associated protein 28 | B | protein | 118 | Saccharomyces cerevisiae | Q02767 (AlphaFold model) |
| Protein SRN2 | C | protein | 192 | Saccharomyces cerevisiae | Q99176 (AlphaFold model) |
| Hypothetical 12.0 kDa protein in ADE3-SER2 intergenic region | D | protein | 79 | Saccharomyces cerevisiae | P42939 (AlphaFold model) |
>2P22_1 Suppressor protein STP22 of temperature-sensitive alpha-factor receptor and arginine permease (chains A) GAMDISPTNHHEMLQNLQTVVNELYREDVDYVADKILTRQTVMQESIARFHEIIAIDKNH LRAVEQAIEQTMHSLNAQIDVLTANRAKVQQFSSTSHVDDEDVNSIAVAKTDGLNQLYNL VAQDYALTDTIECLSRMLHRGTIPLDTFVKQGRELARQQFLVRWHIQRITSPLS
>2P22_2 Vacuolar protein sorting-associated protein 28 (chains B) MQKHNIKLNQNQDISQLFHDEVPLFDNSITSKDKEVIETLSEIYSIVITLDHVEKAYLKD SIDDTQYTNTVDKLLKQFKVYLNSQNKEEINKHFQSIEAFADTYNITASNAITRLERG
>2P22_3 Protein SRN2 (chains C) SRLDIIRAEMDVVPSPGLPEKVNEKSKNIPLPEGINLLSSKEIIDLIQTHRHQLELYVTK FNPLTDFAGKIHAFRDQFKQLEENFEDLHEQKDKVQALLENARILESKYVASWQDYHSEF SKKYGDIALKKKLEQNTKKLDEESSQLETTTRSIDSADDLDQFIKNYLDIRTQYHLRREK LATWDKQGNLKY
>2P22_4 Hypothetical 12.0 kDa protein in ADE3-SER2 intergenic region (chains D) MNVEELLRRIPLYNKYGKDFPQETVTRFQMPEFKLPALQPTRDLLCPWYEECDNITKVCQ LHDSSNKKFDQWYKEQYLS
Molecular architecture and functional model of the complete yeast ESCRT-I heterotetramer. Kostelansky, M.S., Schluter, C., Tam, Y.Y. et al. Cell (2007) 129:485-498. DOI 10.1016/j.cell.2007.03.016 · PubMed
Other PDB entries of the same protein (UniProt P25604 (AlphaFold model), which also has an AlphaFold model), best resolution first:
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