› 1ime

X-ray diffraction
2.25Å resolution

STRUCTURAL STUDIES OF METAL BINDING BY INOSITOL MONOPHOSPHATASE: EVIDENCE FOR TWO-METAL ION CATALYSIS

Released:
DOI: 10.2210/pdb1ime/pdb
PDB entry 1ime coloured by chain, front view.
PDB entry 1ime coloured by chain, side view.
PDB entry 1ime coloured by chain, top view.
Source organism: Homo sapiens
Primary publication:
Structural studies of metal binding by inositol monophosphatase: evidence for two-metal ion catalysis.
Bone R, Frank L, Springer JP, Atack JR
Biochemistry 33 9468-76 (1994)
PMID: 8068621

Function and Biology Details

Reactions catalysed: 
Myo-inositol phosphate + H(2)O = myo-inositol + phosphate
Alpha-D-galactose 1-phosphate + H(2)O = D-galactose + phosphate
Biochemical function:
Biological process:
Cellular component:
Sequence domains:
Structure domain:

Structure analysis Details

Assembly composition:
homo dimer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-151370 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Inositol monophosphatase 1 Chains: A, B
Molecule details ›
Chains: A, B
Length: 277 amino acids
Theoretical weight: 30.22 KDa
Source organism: Homo sapiens
Expression system: Not provided
UniProt:
  • Canonical: P29218 (Residues: 1-277; Coverage: 100%)
Gene names: IMPA, IMPA1
Sequence domains: Inositol monophosphatase family
Structure domains:

Ligands and Environments

1 bound ligand:
Ligand CA 2 x CA
No modified residues

Experiments and Validation Details

Entry percentile scores
Spacegroup: P3221
Unit cell:
a: 86Å b: 86Å c: 154.1Å
α: 90° β: 90° γ: 120°
R-values:
R R work R free
0.184 0.184 not available
Expression system: Not provided

Quick links

Citations

6 review citations

Molecular targets of lithium action.
Phiel et al. (2001)
5 more

7 mentions without citation

LIGSITEcsc: predicting ligand binding sites using the Connolly surface and degree of conservation.
Huang et al. (2006)
6 more