› 5tqs

X-ray diffraction
1.88Å resolution

Phospholipase C gamma-1 C-terminal SH2 domain bound to a phosphopeptide derived from the receptor tyrosine kinase ErbB2

Released:
DOI: 10.2210/pdb5tqs/pdb
PDB entry 5tqs coloured by chain, front view.
PDB entry 5tqs coloured by chain, side view.
PDB entry 5tqs coloured by chain, top view.
Source organisms:
Primary publication:
Multimodal Recognition of Diverse Peptides by the C-Terminal SH2 Domain of Phospholipase C-γ1 Protein.
McKercher MA, Guan X, Tan Z, Wuttke DS
Biochemistry 56 2225-2237 (2017)
PMID: 28376302

Function and Biology Details

Reactions catalysed: 
1-phosphatidyl-1D-myo-inositol 4,5-bisphosphate + H(2)O = 1D-myo-inositol 1,4,5-trisphosphate + diacylglycerol
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-138063 (preferred)
Entry contents:
2 distinct polypeptide molecules
Macromolecules (2 distinct):
1-phosphatidylinositol 4,5-bisphosphate phosphodiesterase gamma-1 Chains: A, B, C, D
Molecule details ›
Chains: A, B, C, D
Length: 101 amino acids
Theoretical weight: 11.99 KDa
Source organism: Bos taurus
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: P08487 (Residues: 663-759; Coverage: 8%)
Gene name: PLCG1
Sequence domains: SH2 domain
Structure domains: SH2 domain
Receptor tyrosine-protein kinase erbB-2 Chains: E, F, G, H
Molecule details ›
Chains: E, F, G, H
Length: 11 amino acids
Theoretical weight: 1.51 KDa
Source organism: Homo sapiens
Expression system: Not provided
UniProt:
  • Canonical: P04626 (Residues: 1218-1228; Coverage: 1%)
Gene names: ERBB2, HER2, MLN19, NEU, NGL

Ligands and Environments

No bound ligands
1 modified residue:
Ligand PTR 4 x PTR

Experiments and Validation Details

Entry percentile scores
X-ray source: ALS BEAMLINE 8.2.1
Spacegroup: P21
Unit cell:
a: 65.32Å b: 30.62Å c: 104.57Å
α: 90° β: 100.12° γ: 90°
R-values:
R R work R free
0.191 0.188 0.237
Expression systems:
  • Escherichia coli BL21(DE3)
  • Not provided

Quick links

Citations

1 review citation

SH2 Domain Binding: Diverse FLVRs of Partnership.
Jaber Chehayeb et al. (2020)
4 other articles