› 1lw3

X-ray diffraction
2.3Å resolution

Crystal Structure of Myotubularin-related protein 2 complexed with phosphate

Released:
DOI: 10.2210/pdb1lw3/pdb
PDB entry 1lw3 coloured by chain, front view.
PDB entry 1lw3 coloured by chain, side view.
PDB entry 1lw3 coloured by chain, top view.
Source organism: Homo sapiens
Primary publication:
Crystal structure of a phosphoinositide phosphatase, MTMR2: insights into myotubular myopathy and Charcot-Marie-Tooth syndrome.
Begley MJ, Taylor GS, Kim SA, Veine DM, Dixon JE, Stuckey JA
Mol Cell 12 1391-402 (2003)
PMID: 14690594

Function and Biology Details

Reaction catalysed: 
1-phosphatidyl-1D-myo-inositol 3,5-bisphosphate + H(2)O = 1-phosphatidyl-1D-myo-inositol 5-phosphate + phosphate
Biochemical function:
Biological process:
Cellular component:
Sequence domains:
Structure domains:

Structure analysis Details

Assembly composition:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-171777 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Phosphatidylinositol-3,5-bisphosphate 3-phosphatase MTMR2 Chain: A
Molecule details ›
Chain: A
Length: 657 amino acids
Theoretical weight: 75.01 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: Q13614 (Residues: 1-643; Coverage: 100%)
Gene names: KIAA1073, MTMR2
Sequence domains:
Structure domains: Pleckstrin-homology domain (PH domain)/Phosphotyrosine-binding domain (PTB)

Ligands and Environments

1 bound ligand:
Ligand PO4 3 x PO4
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: APS BEAMLINE 5ID-B
Spacegroup: P41212
Unit cell:
a: 66.08Å b: 66.08Å c: 261.41Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.25 0.209 0.273
Expression system: Escherichia coli BL21(DE3)

Quick links

Citations

34 review citations

Protein tyrosine phosphatases in the human genome.
Alonso et al. (2004)
33 more

10 mentions without citation

Polyphosphoinositide-Binding Domains: Insights from Peripheral Membrane and Lipid-Transfer Proteins.
Pemberton et al. (2019)
9 more