› 6zk0

X-ray diffraction
1.47Å resolution

1.47A human IMPase with ebselen

Released:
DOI: 10.2210/pdb6zk0/pdb
PDB entry 6zk0 coloured by chain, front view.
PDB entry 6zk0 coloured by chain, side view.
PDB entry 6zk0 coloured by chain, top view.
Source organism: Homo sapiens
Primary publication:
Crystallization and structure of ebselen bound to Cys141 of human inositol monophosphatase.
Fenn GD, Waller-Evans H, Atack JR, Bax BD
Acta Crystallogr F Struct Biol Commun 76 469-476 (2020)
PMID: 33006574

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 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: AAA, BBB
Molecule details ›
Chains: AAA, BBB
Length: 279 amino acids
Theoretical weight: 30.37 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
UniProt:
  • Canonical: P29218 (Residues: 1-277; Coverage: 100%)
Gene names: IMPA, IMPA1
Sequence domains: Inositol monophosphatase family

Ligands and Environments

6 bound ligands:
Ligand NA 8 x NA
Ligand MN 6 x MN
Ligand SO4 2 x SO4
Ligand GOL 9 x GOL
Ligand 9JT 2 x 9JT
Ligand MES 1 x MES
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: DIAMOND BEAMLINE I04-1
Spacegroup: P3221
Unit cell:
a: 84.02Å b: 84.02Å c: 150.22Å
α: 90° β: 90° γ: 120°
R-values:
R R work R free
0.181 0.179 0.208
Expression system: Escherichia coli

Quick links

Citations

3 review citations

Ebselen and Analogues: Pharmacological Properties and Synthetic Strategies for Their Preparation.
Santi et al. (2021)
2 more

1 mention without citation

Crystallization and structure of ebselen bound to Cys141 of human inositol monophosphatase.
Fenn et al. (2020)