3eab

X-ray diffraction
2.5Å resolution

Crystal structure of Spastin MIT in complex with ESCRT III

Released:

Function and Biology Details

Reaction catalysed:
n ATP + n H(2)O + a microtubule = n ADP + n phosphate + (n+1) alpha/beta tubulin heterodimers
Biochemical function:
  • not assigned
Biological process:
  • not assigned
Cellular component:
  • not assigned
Sequence domain:

Structure analysis Details

Assembly composition:
Non-polymer only dimer (preferred)
Entry contents:
2 distinct polypeptide molecules
Macromolecules (2 distinct):
Spastin Chains: A, B, C, D, E, F
Molecule details ›
Chains: A, B, C, D, E, F
Length: 89 amino acids
Theoretical weight: 10.31 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
UniProt:
  • Canonical: Q9UBP0 (Residues: 112-196; Coverage: 14%)
Gene names: ADPSP, FSP2, KIAA1083, SPAST, SPG4
Structure domains: Hypothetical protein 1500032h18.
Charged multivesicular body protein 1b Chains: G, H, I, J, K, L
Molecule details ›
Chains: G, H, I, J, K, L
Length: 50 amino acids
Theoretical weight: 5.42 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
UniProt:
  • Canonical: Q7LBR1 (Residues: 148-197; Coverage: 25%)
Gene names: C18orf2, CHMP1B

Ligands and Environments

No bound ligands
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: APS BEAMLINE 22-ID
Spacegroup: P21212
Unit cell:
a: 151.967Å b: 95.493Å c: 100.36Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.232 0.232 0.268
Expression system: Escherichia coli