› 3tkz

X-ray diffraction
1.8Å resolution

Structure of the SHP-2 N-SH2 domain in a 1:2 complex with RVIpYFVPLNR peptide

Released:
DOI: 10.2210/pdb3tkz/pdb
PDB entry 3tkz coloured by chain, front view.
PDB entry 3tkz coloured by chain, side view.
PDB entry 3tkz coloured by chain, top view.
Source organism: Homo sapiens
Primary publication:
Simultaneous binding of two peptidyl ligands by a SRC homology 2 domain.
Zhang Y, Zhang J, Yuan C, Hard RL, Park IH, Li C, Bell C, Pei D
Biochemistry 50 7637-46 (2011)
PMID: 21800896

Function and Biology Details

Reaction catalysed: 
Protein tyrosine phosphate + H(2)O = protein tyrosine + phosphate
Biochemical function:
  • not assigned
Biological process:
  • not assigned
Cellular component:
  • not assigned
Sequence domains:

Structure analysis Details

Assembly composition:
hetero trimer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-164078 (preferred)
Entry contents:
2 distinct polypeptide molecules
Macromolecules (2 distinct):
Tyrosine-protein phosphatase non-receptor type 11 Chain: A
Molecule details ›
Chain: A
Length: 109 amino acids
Theoretical weight: 12.29 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: Q06124 (Residues: 1-106; Coverage: 18%)
Gene names: PTP2C, PTPN11, SHPTP2
Sequence domains: SH2 domain
Structure domains: SH2 domain
PROTEIN (RVIpYFVPLNR peptide) Chains: P, Q
Molecule details ›
Chains: P, Q
Length: 10 amino acids
Theoretical weight: 1.36 KDa
Source organism: Homo sapiens
Expression system: Not provided

Ligands and Environments

No bound ligands
1 modified residue:
Ligand PTR 2 x PTR

Experiments and Validation Details

Entry percentile scores
X-ray source: APS BEAMLINE 19-BM
Spacegroup: P43212
Unit cell:
a: 62.865Å b: 62.865Å c: 75.322Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.198 0.197 0.216
Expression systems:
  • Escherichia coli BL21(DE3)
  • Not provided

Quick links

Citations

2 review citations

The language of SH2 domain interactions defines phosphotyrosine-mediated signal transduction.
Liu et al. (2012)
1 more

6 mentions without citation

Phosphotyrosine recognition domains: the typical, the atypical and the versatile.
Kaneko et al. (2012)
5 more