2GD5: Budding by the ESCRTIII factor CHMP3

Structural basis for budding by the ESCRTIII factor CHMP3. Determined by X-ray diffraction at 2.8 Å resolution. Released 13 Jun 2006.

Method: X-ray diffraction
Resolution: 2.8 Å
Organism: Homo sapiens
Chains: 4
Atoms: 4,746
Mol. weight: 84.01 kDa
Released: 13 Jun 2006

Explore 2GD5 in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

2GD5 contains 22 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.

Chain A: 5 helices, 0 β-strands

Element	Residues	Length
α-helix	15-53	39
α-helix	57-100	44
α-helix	109-112	4
α-helix	125-137	13
α-helix	164-167	4

Chain B: 6 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
α-helix	164-173	10

Chain C: 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	163-170	8

Chain D: 6 helices, 0 β-strands

Element	Residues	Length
α-helix	9-11	3
α-helix	12-53	42
α-helix	57-100	44
α-helix	109-116	8
α-helix	124-137	14
α-helix	164-173	10

Molecules and chains

Molecule	Chains	Type	Length	Organism	UniProt
Charged multivesicular body protein 3	A, B, C, D	protein	179	Homo sapiens	Q9Y3E7 (AlphaFold model)

Sequence of entity 1 (A, B, C, D), FASTA

>2GD5_1 Charged multivesicular body protein 3 (chains A, B, C, D)
GAMAEKPPKELVNEWSLKIRKEMRVVDRQIRDIQREEEKVKRSVKDAAKKGQKDVCIVLA
KEMIRSRKAVSKLYASKAHMNSVLMGMKNQLAVLRVAGSLQKSTEVMKAMQSLVKIPEIQ
ATMRELSKEMMKAGIIEEMLEDTFESMDDQEEMEEEAEMEIDRILFEITAGALGKAPSK

Primary citation

Structural Basis for Budding by the ESCRT-III Factor CHMP3. Pineda-Molina, E., Ravelli, R.B., Zamborlini, A. et al. Dev Cell (2006) 10:821-830. DOI 10.1016/j.devcel.2006.03.013 · 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
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)
3FRT 4.0 Å, The structure of human CHMP3 (residues 8 - 222).

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