3FRT: Human CHMP3 (residues 8 - 222)

The structure of human CHMP3 (residues 8 - 222). Determined by X-ray diffraction at 4.0 Å resolution. Released 30 Jun 2009.

Method: X-ray diffraction
Resolution: 4.0 Å
Organism: Homo sapiens
Chains: 2
Atoms: 2,270
Mol. weight: 49.4 kDa
Released: 30 Jun 2009

Explore 3FRT in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

3FRT contains 10 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.

Chains A and B: 5 helices, 0 β-strands

Element	Residues	Length
α-helix	13-53	41
α-helix	57-96	40
α-helix	108-116	9
α-helix	121-137	17
α-helix	164-170	7

Molecules and chains

Molecule	Chains	Type	Length	Organism	UniProt
Charged multivesicular body protein 3	A, B	protein	218	Homo sapiens	Q9Y3E7 (AlphaFold model)

Sequence of entity 1 (A, B), FASTA

>3FRT_1 Charged multivesicular body protein 3 (chains A, B)
GHMQEKPPKELVNEWSLKIRKEMRVVDRQIRDIQREEEKVKRSVKDAAKKGQKDVCIVLA
KEMIRSRKAVSKLYASKAHMNSVLMGMKNQLAVLRVAGSLQKSTEVMKAMQSLVKIPEIQ
ATMRELSKEMMKAGIIEEMLEDTFESMDDQEEMEEEAEMEIDRILFEITAGALGKAPSKV
TDALPEPEPPGAMAASEDEEEEEEALEAMQSRLATLRS

Primary citation

Structural basis for ESCRT-III protein autoinhibition. Bajorek, M., Schubert, H.L., McCullough, J. et al. Nat Struct Mol Biol (2009) 16:754-762. DOI 10.1038/nsmb.1621 · PubMed

Other PDB entries of the same protein (UniProt Q9Y3E7 (AlphaFold model), which also has an AlphaFold model), best resolution first:

2XZE 1.75 Å, Structural basis for AMSH-ESCRT-III CHMP3 interaction
2GD5 2.8 Å, Structural basis for budding by the ESCRTIII factor CHMP3
7ZCG 3.3 Å, CHMP2A-CHMP3 heterodimer (430 Angstrom diameter)
7ZCH 3.6 Å, CHMP2A-CHMP3 heterodimer (410 Angstrom diameter)
3FRV 3.7 Å, Structure of Human CHMP3 (residues 1-150)

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