› 5iky

X-ray diffraction
2.5Å resolution

Apo structure of Obc1, a bifunctional enzyme for quorum sensing-dependent oxalogenesis

Released:
DOI: 10.2210/pdb5iky/pdb
PDB entry 5iky coloured by chain, front view.
PDB entry 5iky coloured by chain, side view.
PDB entry 5iky coloured by chain, top view.
Source organism: Burkholderia thailandensis E264
Primary publication:
Structural Insights into an Oxalate-producing Serine Hydrolase with an Unusual Oxyanion Hole and Additional Lyase Activity.
Oh J, Hwang I, Rhee S
J Biol Chem 291 15185-95 (2016)
PMID: 27226606

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-165809 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Oxalate biosynthetic component 1 Chain: A
Molecule details ›
Chain: A
Length: 1125 amino acids
Theoretical weight: 124.42 KDa
Source organism: Burkholderia thailandensis E264
Expression system: Escherichia coli BL21(DE3)

Ligands and Environments

1 bound ligand:
Ligand MG 1 x MG
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: PAL/PLS BEAMLINE 7A (6B, 6C1)
Spacegroup: R32
Unit cell:
a: 230.81Å b: 230.81Å c: 253.732Å
α: 90° β: 90° γ: 120°
R-values:
R R work R free
0.199 0.198 0.227
Expression system: Escherichia coli BL21(DE3)

Quick links

Citations

3 citation in other articles

Proteomic Profiling of Burkholderia thailandensis During Host Infection Using Bio-Orthogonal Noncanonical Amino Acid Tagging (BONCAT).
Franco et al. (2018)
2 more

1 mention without citation

Structural Insights into an Oxalate-producing Serine Hydrolase with an Unusual Oxyanion Hole and Additional Lyase Activity.
Oh et al. (2016)