3FRV: Human CHMP3

Structure of Human CHMP3 (residues 1-150). Determined by X-ray diffraction at 3.7 Å resolution. Released 30 Jun 2009.

Method: X-ray diffraction
Resolution: 3.7 Å
Organism: Homo sapiens
Chains: 1
Atoms: 1,053
Mol. weight: 17.41 kDa
Released: 30 Jun 2009

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

Secondary structure: helices and β-sheets

3FRV contains 5 α-helices and 0 β-strands across 1 chain. 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.

Chain A: 5 helices, 0 β-strands

Element	Residues	Length
α-helix	10-12	3
α-helix	15-53	39
α-helix	57-100	44
α-helix	109-116	8
α-helix	126-137	12

Molecules and chains

Molecule	Chains	Type	Length	Organism	UniProt
Charged multivesicular body protein 3	A	protein	152	Homo sapiens	Q9Y3E7 (AlphaFold model)

Sequence of entity 1 (A), FASTA

>3FRV_1 Charged multivesicular body protein 3 (chains A)
GHMGLFGKTQEKPPKELVNEWSLKIRKEMRVVDRQIRDIQREEEKVKRSVKDAAKKGQKD
VCIVLAKEMIRSRKAVSKLYASKAHMNSVLMGMKNQLAVLRVAGSLQKSTEVMKAMQSLV
KIPEIQATMRELSKEMMKAGIIEEMLEDTFES

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)
3FRT 4.0 Å, The structure of human CHMP3 (residues 8 - 222).

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