› 1m7r

X-ray diffraction
2.6Å resolution

Crystal Structure of Myotubularin-related Protein-2 (MTMR2) Complexed with Phosphate

Released:
DOI: 10.2210/pdb1m7r/pdb
PDB entry 1m7r coloured by chain, front view.
PDB entry 1m7r coloured by chain, side view.
PDB entry 1m7r 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

Reactions catalysed: 
1-phosphatidyl-1D-myo-inositol 3-phosphate + H(2)O = 1-phosphatidyl-1D-myo-inositol + phosphate
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:
homo dimer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-171778 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Myotubularin-related protein 2 Chains: A, B
Molecule details ›
Chains: A, B
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 4 x PO4
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: APS BEAMLINE 5ID-B
Spacegroup: C2
Unit cell:
a: 158.25Å b: 82.66Å c: 100.13Å
α: 90° β: 117.93° γ: 90°
R-values:
R R work R free
0.207 0.207 0.28
Expression system: Escherichia coli BL21(DE3)

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Citations

34 review citations

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

2 mentions without citation

Structural mechanisms of plant glucan phosphatases in starch metabolism.
Meekins et al. (2016)
1 more