› 5ul4

X-ray diffraction
1.85Å resolution

Structure of Cobalamin-dependent S-adenosylmethionine radical enzyme OxsB with aqua-cobalamin and S-adenosylmethionine bound

Released:
DOI: 10.2210/pdb5ul4/pdb
PDB entry 5ul4 coloured by chain, front view.
PDB entry 5ul4 coloured by chain, side view.
PDB entry 5ul4 coloured by chain, top view.
Source organism: Priestia megaterium
Primary publication:
A B12-dependent radical SAM enzyme involved in oxetanocin A biosynthesis.
Bridwell-Rabb J, Zhong A, Sun HG, Drennan CL, Liu HW
OpenAccess logo Nature 544 322-326 (2017)
PMID: 28346939

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-127682 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
4'-phospho-dehydrooxetanocin synthase Chain: A
Molecule details ›
Chain: A
Length: 744 amino acids
Theoretical weight: 86.68 KDa
Source organism: Priestia megaterium
Expression system: Escherichia coli
UniProt:
  • Canonical: O24770 (Residues: 1-744; Coverage: 100%)
Gene name: oxsB
Sequence domains: Radical SAM superfamily

Ligands and Environments

5 bound ligands:
Ligand SF4 1 x SF4
Ligand B12 1 x B12
Ligand SAM 1 x SAM
Ligand MES 1 x MES
Ligand EDO 15 x EDO
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: APS BEAMLINE 24-ID-C
Spacegroup: P212121
Unit cell:
a: 89.36Å b: 99.6Å c: 121.44Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.195 0.192 0.231
Expression system: Escherichia coli

Quick links

Citations

13 review citations

Formation and Cleavage of C-C Bonds by Enzymatic Oxidation-Reduction Reactions.
Guengerich et al. (2018)
12 more

6 mentions without citation

Enzymatic assembly of carbon-carbon bonds via iron-catalysed sp3 C-H functionalization.
Zhang et al. (2019)
5 more