Crystal Structure of CHMP4B hairpin. Determined by X-ray diffraction at 1.8 Å resolution. Released 9 May 2012.
Explore 4ABM in 3D Show helices and sheets RCSB PDB PDBe
4ABM contains 8 α-helices and 0 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 | 20-57 | 38 | |
| α-helix | 62-96 | 35 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| α-helix | 20-56 | 37 | |
| α-helix | 64-95 | 32 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| α-helix | 22-55 | 34 | |
| α-helix | 62-94 | 33 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| Charged multivesicular body protein 4B | A, B, C, D | protein | 79 | HOMO SAPIENS | Q9H444 (AlphaFold model) |
>4ABM_1 CHARGED MULTIVESICULAR BODY PROTEIN 4B (chains A, B, C, D) GAMEQEAIQRLRDTEEMLSKKQEFLEKKIEQELTAAKKHGTKNKRAALQALKRKKRYEKQ LAQIDGTLSTIEFQREALE
Cc2D1A is a Regulator of Escrt-III Chmp4B. Martinelli, N., Hartlieb, B., Usami, Y. et al. J Mol Biol (2012) 419:75. DOI 10.1016/J.JMB.2012.02.044 · PubMed
Other PDB entries of the same protein (UniProt Q9H444 (AlphaFold model), which also has an AlphaFold model), best resolution first:
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