2mc1

Solution NMR

Solution structure of the Vav1 SH2 domain complexed with a Syk-derived singly phosphorylated peptide

Released:

Function and Biology Details

Reaction catalysed:
ATP + a [protein]-L-tyrosine = ADP + a [protein]-L-tyrosine phosphate
Biochemical function:
  • not assigned
Biological process:
  • not assigned
Cellular component:
  • not assigned

Structure analysis Details

Assembly composition:
hetero dimer (preferred)
PDBe Complex ID:
PDB-CPX-147390 (preferred)
Entry contents:
2 distinct polypeptide molecules
Macromolecules (2 distinct):
Proto-oncogene vav Chain: A
Molecule details ›
Chain: A
Length: 107 amino acids
Theoretical weight: 12.34 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
UniProt:
  • Canonical: P15498 (Residues: 664-767; Coverage: 12%)
Gene names: VAV, VAV1
Sequence domains: SH2 domain
Structure domains: SH2 domain
Tyrosine-protein kinase SYK Chain: B
Molecule details ›
Chain: B
Length: 13 amino acids
Theoretical weight: 1.59 KDa
Source organism: Mus musculus
Expression system: Not provided
UniProt:
  • Canonical: P48025 (Residues: 338-350; Coverage: 2%)
Gene names: Syk, Sykb, ptk72

Ligands and Environments

No bound ligands
1 modified residue:

Experiments and Validation Details

Entry percentile scores
Chemical shift assignment: 73%
Refinement method: simulated annealing
Expression systems:
  • Escherichia coli
  • Not provided