› 3frv

X-ray diffraction
3.7Å resolution

Structure of Human CHMP3 (residues 1-150)

Released:
DOI: 10.2210/pdb3frv/pdb
PDB entry 3frv coloured by chain, front view.
PDB entry 3frv coloured by chain, side view.
PDB entry 3frv coloured by chain, top view.
Source organism: Homo sapiens
Primary publication:
Structural basis for ESCRT-III protein autoinhibition.
Bajorek M, Schubert HL, McCullough J, Langelier C, Eckert DM, Stubblefield WM, Uter NT, Myszka DG, Hill CP, Sundquist WI
Nat Struct Mol Biol 16 754-62 (2009)
PMID: 19525971

Function and Biology Details

Biochemical function:
  • not assigned
Biological process:
Cellular component:
  • not assigned
Sequence domain:

Structure analysis Details

Assembly composition:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-195206 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Charged multivesicular body protein 3 Chain: A
Molecule details ›
Chain: A
Length: 152 amino acids
Theoretical weight: 17.41 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
UniProt:
  • Canonical: Q9Y3E7 (Residues: 1-150; Coverage: 68%)
Gene names: CGI-149, CGI149, CHMP3, NEDF, VPS24
Sequence domains: Snf7

Ligands and Environments

No bound ligands
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: RIGAKU MICROMAX-007 HF
Spacegroup: P61
Unit cell:
a: 111.484Å b: 111.484Å c: 30.567Å
α: 90° β: 90° γ: 120°
R-values:
R R work R free
0.41 0.435 0.375
Expression system: Escherichia coli

Quick links

Citations

41 review citations

The ESCRT pathway.
Henne et al. (2011)
40 more

3 mentions without citation

Structural basis for ESCRT-III protein autoinhibition.
Bajorek et al. (2009)
2 more