1wr0

Solution NMR

Structural characterization of the MIT domain from human Vps4b

Released:
Source organism: Homo sapiens
Primary publication:
Structural characterization of the MIT domain from human Vps4b.
Biochem Biophys Res Commun 334 460-5 (2005)
PMID: 16018968

Function and Biology Details

Reaction catalysed:
ATP + H(2)O = ADP + phosphate
Biochemical function:
  • not assigned
Biological process:
  • not assigned
Cellular component:
  • not assigned
Structure domain:

Structure analysis Details

Assembly composition:
monomeric (preferred)
PDBe Complex ID:
PDB-CPX-130908 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Vacuolar protein sorting-associated protein 4B Chain: A
Molecule details ›
Chain: A
Length: 81 amino acids
Theoretical weight: 9.21 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: O75351 (Residues: 1-77; Coverage: 17%)
Gene names: MIG1, SKD1, VPS42, VPS4B
Sequence domains: MIT (microtubule interacting and transport) domain
Structure domains: Phosphotransferase system, lactose/cellobiose-type IIA subunit

Ligands and Environments

No bound ligands
No modified residues

Experiments and Validation Details

Entry percentile scores
Refinement method: torsion angle dynamics, simulated annealing, molecular dynamics, energy minimization
Expression system: Escherichia coli BL21(DE3)