PDBe 2mcn

Solution NMR

Distinct ubiquitin binding modes exhibited by SH3 domains: molecular determinants and functional implications

Released:

Function and Biology Details

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

Structure analysis Details

Assembly composition:
hetero dimer (preferred)
Entry contents:
2 distinct polypeptide molecules
Macromolecules (2 distinct):
CD2-associated protein Chain: A
Molecule details ›
Chain: A
Length: 61 amino acids
Theoretical weight: 7.28 KDa
Source organism: Mus musculus
Expression system: Escherichia coli
UniProt:
  • Canonical: Q9JLQ0 (Residues: 2-62; Coverage: 10%)
Gene names: Cd2ap, Mets1
Sequence domains: Variant SH3 domain
Structure domains: SH3 Domains
Ubiquitin Chain: B
Molecule details ›
Chain: B
Length: 76 amino acids
Theoretical weight: 8.58 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
UniProt:
  • Canonical: P0CG48 (Residues: 609-684; Coverage: 11%)
Gene name: UBC
Sequence domains: Ubiquitin family
Structure domains: Phosphatidylinositol 3-kinase Catalytic Subunit; Chain A, domain 1

Ligands and Environments

No bound ligands

No modified residues

Experiments and Validation Details

Entry percentile scores
Chemical shift assignment: 15%
Refinement method: simulated annealing, molecular dynamics, docking, simulated annealing, molecular dynamics
Chemical shifts: BMR19447  
Expression system: Escherichia coli