2F66: ESCRT-I endosomal trafficking complex
Structure of the ESCRT-I endosomal trafficking complex. Determined by X-ray diffraction at 2.8 Å resolution. Released 18 Apr 2006.
- Method
- X-ray diffraction
- Resolution
- 2.8 Å
- Organism
- Saccharomyces cerevisiae
- Chains
- 6
- Atoms
- 3,976
- Mol. weight
- 61.55 kDa
- Released
- 18 Apr 2006
Explore 2F66 in 3D
Show helices and sheets
RCSB PDB
PDBe
Secondary structure: helices and β-sheets
2F66 contains 19 α-helices and 0 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: 2 helices, 0 β-strands
| Element | Residues | Length | Sheet |
|---|
| α-helix | 323-350 | 28 | |
| α-helix | 356-380 | 25 | |
Chain B: 6 helices, 0 β-strands
| Element | Residues | Length | Sheet |
|---|
| α-helix | 21-23 | 3 | |
| α-helix | 31-58 | 28 | |
| α-helix | 64-82 | 19 | |
| α-helix | 87-100 | 14 | |
| α-helix | 108-116 | 9 | |
| α-helix | 119-121 | 3 | |
Chain C: 2 helices, 0 β-strands
| Element | Residues | Length | Sheet |
|---|
| α-helix | 145-171 | 27 | |
| α-helix | 178-202 | 25 | |
Chain D: 2 helices, 0 β-strands
| Element | Residues | Length | Sheet |
|---|
| α-helix | 323-350 | 28 | |
| α-helix | 356-381 | 26 | |
Chain E: 5 helices, 0 β-strands
| Element | Residues | Length | Sheet |
|---|
| α-helix | 31-59 | 29 | |
| α-helix | 64-81 | 18 | |
| α-helix | 87-100 | 14 | |
| α-helix | 108-117 | 10 | |
| α-helix | 119-121 | 3 | |
Chain F: 2 helices, 0 β-strands
| Element | Residues | Length | Sheet |
|---|
| α-helix | 146-170 | 25 | |
| α-helix | 180-203 | 24 | |
Molecules and chains
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|
| Suppressor protein STP22 of temperature-sensitive alpha-factor receptor and arginine permease | A, D | protein | 65 | Saccharomyces cerevisiae | P25604 (AlphaFold model) |
| Vacuolar protein sorting-associated protein VPS28 | B, E | protein | 116 | Saccharomyces cerevisiae | Q02767 (AlphaFold model) |
| Protein SRN2 | C, F | protein | 82 | Saccharomyces cerevisiae | Q99176 (AlphaFold model) |
Sequence of entity 1 (A, D), FASTA
>2F66_1 Suppressor protein STP22 of temperature-sensitive alpha-factor receptor and arginine permease (chains A, D)
MTDGLNQLYNLVAQDYALTDTIEALSRMLHRGTIPLDTFVKQGRELARQQFLVRWHIQRI
TSPLS
Sequence of entity 2 (B, E), FASTA
>2F66_2 Vacuolar protein sorting-associated protein VPS28 (chains B, E)
GAMDISQLFHDEVPLFDNSITSKDKEVIETLSEIYSIVITLDHVEKAYLKDSIDDTQYTN
TVDKLLKQFKVYLNSQNKEEINKHFQSIEAFADTYNITASNAITRLERGIPITAEH
Sequence of entity 3 (C, F), FASTA
>2F66_3 Protein SRN2 (chains C, F)
ASWQDYHSEFSKKYGDIALKKKLEQNTKKLDEESSQLETTTRSIDSADDLDQFIKNYLDI
RTQYHLRREKLATWDKQGNLKY
Primary citation
Structural and functional organization of the ESCRT-I trafficking complex. Kostelansky, M.S., Sun, J., Lee, S. et al. Cell (2006) 125:113-126. DOI 10.1016/j.cell.2006.01.049 · PubMed
Other PDB entries of the same protein (UniProt P25604 (AlphaFold model), which also has an AlphaFold model), best resolution first:
- 3R3Q 1.45 Å, Crystal structure of the yeast Vps23 UEV domain
- 1UZX 1.85 Å, A complex of the Vps23 UEV with ubiquitin
- 3R42 1.87 Å, Crystal structure of the yeast vps23 UEV domain in complex with a vps27 PSDP peptide
- 2F6M 2.1 Å, Structure of a Vps23-C:Vps28-N subcomplex
- 2P22 2.7 Å, Structure of the Yeast ESCRT-I Heterotetramer Core
- 2CAZ 3.6 Å, ESCRT-I core
Browse structure collections
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