2xze

X-ray diffraction
1.75Å resolution

Structural basis for AMSH-ESCRT-III CHMP3 interaction

Released:

Function and Biology Details

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

Structure analysis Details

Assembly composition:
hetero dimer (preferred)
Entry contents:
2 distinct polypeptide molecules
Macromolecules (2 distinct):
STAM-binding protein Chains: A, B
Molecule details ›
Chains: A, B
Length: 146 amino acids
Theoretical weight: 17.16 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
UniProt:
  • Canonical: O95630 (Residues: 1-146; Coverage: 34%)
Gene names: AMSH, STAMBP
Sequence domains: USP8 dimerisation domain
Structure domains: Phosphotransferase system, lactose/cellobiose-type IIA subunit
Charged multivesicular body protein 3 Chains: Q, R
Molecule details ›
Chains: Q, R
Length: 40 amino acids
Theoretical weight: 4.33 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
UniProt:
  • Canonical: Q9Y3E7 (Residues: 183-222; Coverage: 18%)
Gene names: CGI-149, CGI149, CHMP3, NEDF, VPS24

Ligands and Environments

No bound ligands
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: ESRF BEAMLINE ID14-4
Spacegroup: P41
Unit cell:
a: 45.97Å b: 45.97Å c: 206.91Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.193 0.192 0.227
Expression system: Escherichia coli