› 6kc4

X-ray diffraction
1.37Å resolution

Crystal structure of human Fer SH2 domain bound to a phosphopeptide (DEpYENVD)

Released:
DOI: 10.2210/pdb6kc4/pdb
PDB entry 6kc4 coloured by chain, front view.
PDB entry 6kc4 coloured by chain, side view.
PDB entry 6kc4 coloured by chain, top view.
Source organisms:
Primary publication:
High-resolution structural analysis shows how different crystallographic environments can induce alternative modes of binding of a phosphotyrosine peptide to the SH2 domain of Fer tyrosine kinase.
Matsuura Y
Protein Sci 28 2011-2019 (2019)
PMID: 31441171

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
Sequence domains:

Structure analysis Details

Assembly composition:
hetero dimer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-147774 (preferred)
Entry contents:
2 distinct polypeptide molecules
Macromolecules (2 distinct):
Tyrosine-protein kinase Fer Chains: A, C, E, G, I, K
Molecule details ›
Chains: A, C, E, G, I, K
Length: 102 amino acids
Theoretical weight: 11.74 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
UniProt:
  • Canonical: P16591 (Residues: 453-552; Coverage: 12%)
Gene names: FER, TYK3
Sequence domains: SH2 domain
phosphopeptide (EDpYENVD) Chains: B, D, F, H, J, L
Molecule details ›
Chains: B, D, F, H, J, L
Length: 7 amino acids
Theoretical weight: 963 Da
Source organism: synthetic construct
Expression system: Not provided

Ligands and Environments

No bound ligands
1 modified residue:
Ligand PTR 6 x PTR

Experiments and Validation Details

Entry percentile scores
X-ray source: PHOTON FACTORY BEAMLINE BL-17A
Spacegroup: P21
Unit cell:
a: 34.7Å b: 186.661Å c: 50.58Å
α: 90° β: 96.96° γ: 90°
R-values:
R R work R free
0.166 0.165 0.186
Expression systems:
  • Escherichia coli
  • Not provided

Quick links

Citations

1 mention without citation

High-resolution structural analysis shows how different crystallographic environments can induce alternative modes of binding of a phosphotyrosine peptide to the SH2 domain of Fer tyrosine kinase.
Matsuura Y. (2019)