› 4grz

X-ray diffraction
1.37Å resolution

Crystal structure of SHP1 catalytic domain with PO4

Released:
DOI: 10.2210/pdb4grz/pdb
PDB entry 4grz coloured by chain, front view.
PDB entry 4grz coloured by chain, side view.
PDB entry 4grz coloured by chain, top view.
Source organism: Homo sapiens
Primary publication:
Structure-guided studies of the SHP-1/JAK1 interaction provide new insights into phosphatase catalytic domain substrate recognition.
Alicea-Velázquez NL, Jakoncic J, Boggon TJ
J Struct Biol 181 243-51 (2013)
PMID: 23296072

Function and Biology Details

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

Structure analysis Details

Assembly composition:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-151411 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Tyrosine-protein phosphatase non-receptor type 6 Chain: A
Molecule details ›
Chain: A
Length: 288 amino acids
Theoretical weight: 32.92 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: P29350 (Residues: 243-528; Coverage: 48%)
Gene names: HCP, PTP1C, PTPN6
Sequence domains: Protein-tyrosine phosphatase
Structure domains: Protein tyrosine phosphatase superfamily

Ligands and Environments

1 bound ligand:
Ligand PO4 1 x PO4
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: NSLS BEAMLINE X6A
Spacegroup: C2
Unit cell:
a: 164.141Å b: 45.404Å c: 44.679Å
α: 90° β: 91.24° γ: 90°
R-values:
R R work R free
0.17 0.168 0.189
Expression system: Escherichia coli BL21(DE3)

Quick links

Citations

3 review citations

The molecular regulation of Janus kinase (JAK) activation.
Babon et al. (2014)
2 more

3 mentions without citation

Structure-guided studies of the SHP-1/JAK1 interaction provide new insights into phosphatase catalytic domain substrate recognition.
Alicea-Velázquez et al. (2013)
2 more