6TZA: IST1 homolog

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.

Method
Electron microscopy
Resolution
7.2 Å
Organism
Homo sapiens
Chains
14
Atoms
19,432
Mol. weight
301.65 kDa
Released
8 Apr 2020

Explore 6TZA in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

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.

Chains A, B, C, D, E, F, G, H, I, J, K, L, M and N: 12 helices, 0 β-strands

ElementResiduesLengthSheet
α-helix8-4538
α-helix49-8133
α-helix83-886
α-helix94-963
α-helix97-11014
α-helix116-12712
α-helix136-1405
α-helix141-1433
α-helix146-1516
α-helix156-1583
α-helix159-17315
α-helix181-1855

Molecules and chains

MoleculeChainsTypeLengthOrganismUniProt
IST1 homologA, B, C, D, E, F, G, H, I, J, K, L, M, Nprotein189Homo sapiensP53990 (AlphaFold model)
Sequence of entity 1 (A, B, C, D, E, F, G, H, I, J, K, L, M, N), FASTA
>6TZA_1 IST1 homolog (chains A, B, C, D, E, F, G, H, I, J, K, L, M, N)
MLGSGFKAERLRVNLELVINRLKLLEEKKTELAQKARKEIADYLAAGKDERARIRVEHII
REDYLVEAMEILELYCDLLLARFGLIQSMKELDSGLAESVSTLIWAAPRLQSEVAELKIV
ADQLCAKYSKEYGKLCRTNQIGTVNDRLMHKLSVEAPPKILVERYLIEIAKNYNVPYEPD
SVVMAEAPP

Primary citation

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:

Browse structure collections

About this viewer

MolViewer shows 6TZA directly in your browser with nothing to install. Switch between cartoon, ball-and-stick, spacefill and surface views, color by chain, secondary structure or B-factor, measure distances, angles and dihedrals, and share or embed the view.