› 5tk9

X-ray diffraction
1.84Å resolution

Structure of the HD-domain phosphohydrolase OxsA with Oxetanocin-A bound

Released:
DOI: 10.2210/pdb5tk9/pdb
PDB entry 5tk9 coloured by chain, front view.
PDB entry 5tk9 coloured by chain, side view.
PDB entry 5tk9 coloured by chain, top view.
Source organism: Priestia megaterium
Primary publication:
An HD domain phosphohydrolase active site tailored for oxetanocin-A biosynthesis.
Bridwell-Rabb J, Kang G, Zhong A, Liu HW, Drennan CL
Proc Natl Acad Sci U S A 113 13750-13755 (2016)
PMID: 27849620

Function and Biology Details

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

Structure analysis Details

Assembly composition:
homo dimer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-127681 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
4'-phosphooxetanocin A phosphatase Chain: A
Molecule details ›
Chain: A
Length: 194 amino acids
Theoretical weight: 22.71 KDa
Source organism: Priestia megaterium
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: O24769 (Residues: 1-194; Coverage: 100%)
Gene name: oxsA
Sequence domains: HD domain
Structure domains: Hypothetical protein af1432

Ligands and Environments

2 bound ligands:
Ligand MG 1 x MG
Ligand 7D7 1 x 7D7
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: APS BEAMLINE 24-ID-C
Spacegroup: R32
Unit cell:
a: 143.031Å b: 143.031Å c: 53.786Å
α: 90° β: 90° γ: 120°
R-values:
R R work R free
0.182 0.18 0.223
Expression system: Escherichia coli BL21(DE3)

Quick links

Citations

4 review citations

C-C bond forming radical SAM enzymes involved in the construction of carbon skeletons of cofactors and natural products.
Yokoyama et al. (2018)
3 more

1 mention without citation

An HD domain phosphohydrolase active site tailored for oxetanocin-A biosynthesis.
Bridwell-Rabb et al. (2016)