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:
hetero dimer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-181644 (preferred)
Entry contents:
2 distinct polypeptide molecules
Macromolecules (2 distinct):
Spastin
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:
Structure domains: Phosphotransferase system, lactose/cellobiose-type IIA subunit
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%)
Structure domains: Phosphotransferase system, lactose/cellobiose-type IIA subunit
Charged multivesicular body protein 1b
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:
Structure domains: Single alpha-helices involved in coiled-coils or other helix-helix interfaces
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%)
Structure domains: Single alpha-helices involved in coiled-coils or other helix-helix interfaces
Ligands and Environments
No bound ligands
No modified residues
Experiments and Validation Details
X-ray source:
APS BEAMLINE 22-ID
Spacegroup:
P21212
Expression system: Escherichia coli
