CryoEM reconstruction of ESCRT-III filament composed of IST1 NTD R16E K27E double mutant. Determined by electron microscopy at 7.2 Å resolution. Released 8 Apr 2020.
Explore 6TZA in 3D Show helices and sheets RCSB PDB PDBe
6TZA contains 168 α-helices and 0 β-strands across 14 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 | 8-45 | 38 | |
| α-helix | 49-81 | 33 | |
| α-helix | 83-88 | 6 | |
| α-helix | 94-96 | 3 | |
| α-helix | 97-110 | 14 | |
| α-helix | 116-127 | 12 | |
| α-helix | 136-140 | 5 | |
| α-helix | 141-143 | 3 | |
| α-helix | 146-151 | 6 | |
| α-helix | 156-158 | 3 | |
| α-helix | 159-173 | 15 | |
| α-helix | 181-185 | 5 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| IST1 homolog | A, B, C, D, E, F, G, H, I, J, K, L, M, N | protein | 189 | Homo sapiens | P53990 (AlphaFold model) |
>6TZA_1 IST1 homolog (chains A, B, C, D, E, F, G, H, I, J, K, L, M, N) MLGSGFKAERLRVNLELVINRLKLLEEKKTELAQKARKEIADYLAAGKDERARIRVEHII REDYLVEAMEILELYCDLLLARFGLIQSMKELDSGLAESVSTLIWAAPRLQSEVAELKIV ADQLCAKYSKEYGKLCRTNQIGTVNDRLMHKLSVEAPPKILVERYLIEIAKNYNVPYEPD SVVMAEAPP
Membrane constriction and thinning by sequential ESCRT-III polymerization. Nguyen, H.C., Talledge, N., McCullough, J. et al. Nat Struct Mol Biol (2020) 27:392-399. DOI 10.1038/s41594-020-0404-x · PubMed
Other PDB entries of the same protein (UniProt P53990 (AlphaFold model), which also has an AlphaFold model), best resolution first:
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