› 2xmo

X-ray diffraction
1.7Å resolution

The crystal structure of Lmo2642

Released:
DOI: 10.2210/pdb2xmo/pdb
PDB entry 2xmo coloured by chain, front view.
PDB entry 2xmo coloured by chain, side view.
PDB entry 2xmo coloured by chain, top view.
Source organism: Listeria monocytogenes
Primary publication:
Structural and functional analysis of the Lmo2642 cyclic nucleotide phosphodiesterase from Listeria monocytogenes.
Kim YG, Jeong JH, Ha NC, Kim KJ
Proteins 79 1205-14 (2011)
PMID: 21246635

Function and Biology Details

Biochemical function:
Biological process:
  • not assigned
Cellular component:
  • not assigned
Sequence domains:

Structure analysis Details

Assembly composition:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-186935 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Metallophosphoesterase Chains: A, B
Molecule details ›
Chains: A, B
Length: 443 amino acids
Theoretical weight: 49.28 KDa
Source organism: Listeria monocytogenes
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: Q8Y432 (Residues: 1-443; Coverage: 100%)
Gene name: lmo2642
Sequence domains:
Structure domains:

Ligands and Environments

4 bound ligands:
Ligand MN 2 x MN
Ligand FE 2 x FE
Ligand CA 2 x CA
Ligand PO4 2 x PO4
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: PAL/PLS BEAMLINE 4A
Spacegroup: P21
Unit cell:
a: 62.963Å b: 103.267Å c: 73.765Å
α: 90° β: 102.8° γ: 90°
R-values:
R R work R free
0.212 0.212 0.242
Expression system: Escherichia coli BL21(DE3)

Quick links

Citations

1 review citation

Metallophosphoesterases: structural fidelity with functional promiscuity.
Matange et al. (2015)
7 other articles

1 mention without citation

The non-catalytic "cap domain" of a mycobacterial metallophosphoesterase regulates its expression and localization in the cell.
Matange et al. (2014)