CHMP2A-CHMP3 heterodimer (410 Angstrom diameter). Determined by electron microscopy at 3.6 Å resolution. Released 18 Jan 2023.
Explore 7ZCH in 3D Show helices and sheets RCSB PDB PDBe
7ZCH contains 7 α-helices and 0 β-strands across 2 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 | 12-53 | 42 | |
| α-helix | 58-115 | 58 | |
| α-helix | 120-148 | 29 | |
| α-helix | 155-168 | 14 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| α-helix | 11-50 | 40 | |
| α-helix | 58-114 | 57 | |
| α-helix | 119-150 | 32 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| Charged multivesicular body protein 2a | B | protein | 147 | Homo sapiens | O43633 (AlphaFold model) |
| Charged multivesicular body protein 3 | A | protein | 159 | Homo sapiens | Q9Y3E7 (AlphaFold model) |
>7ZCH_1 Charged multivesicular body protein 2a (chains B) RKTPEELLRQNQRALNRAMRELDRERQKLETQEKKIIADIKKMAKQGQMDAVRIMAKDLV RTRRYVRKFVLMRANIQAVSLKIQTLKSNNSMAQAMKGVTKAMGTMNRQLKLPQIQKIMM EFERQAEIMDMKEEMMNDAIDDAMGDE
>7ZCH_2 Charged multivesicular body protein 3 (chains A) PPKELVNEWSLKIRKEMRVVDRQIRDIQREEEKVKRSVKDAAKKGQKDVCIVLAKEMIRS RKAVSKLYASKAHMNSVLMGMKNQLAVLRVAGSLQKSTEVMKAMQSLVKIPEIQATMREL SKEMMKAGIIEEMLEDTFESMDDQEEMEEEAEMEIDRIL
Structural basis of CHMP2A-CHMP3 ESCRT-III polymer assembly and membrane cleavage. Azad, K., Guilligay, D., Boscheron, C. et al. Nat Struct Mol Biol (2023) 30:81-90. DOI 10.1038/s41594-022-00867-8 · PubMed
Other PDB entries of the same protein (UniProt O43633 (AlphaFold model), which also has an AlphaFold model), best resolution first:
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