› 5ybq

X-ray diffraction
2.25Å resolution

Fe(II)/(alpha)ketoglutarate-dependent dioxygenase PrhA-V150L/A232S in complex with preaustinoid A2

Released:
DOI: 10.2210/pdb5ybq/pdb
PDB entry 5ybq coloured by chain, front view.
PDB entry 5ybq coloured by chain, side view.
PDB entry 5ybq coloured by chain, top view.
Source organism: Penicillium brasilianum
Primary publication:
Structure function and engineering of multifunctional non-heme iron dependent oxygenases in fungal meroterpenoid biosynthesis.
Nakashima Y, Mori T, Nakamura H, Awakawa T, Hoshino S, Senda M, Senda T, Abe I
OpenAccess logo Nat Commun 9 104 (2018)
PMID: 29317628

Function and Biology Details

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

Structure analysis Details

Assembly composition:
homo dimer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-495643 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Multifunctional dioxygenase prhA Chains: A, B
Molecule details ›
Chains: A, B
Length: 314 amino acids
Theoretical weight: 35.2 KDa
Source organism: Penicillium brasilianum
Expression system: Escherichia coli
UniProt:
  • Canonical: A0A1E1FFL0 (Residues: 6-294; Coverage: 96%)
Gene name: prhA
Sequence domains: Phytanoyl-CoA dioxygenase (PhyH)

Ligands and Environments

3 bound ligands:
Ligand FE 2 x FE
Ligand AKG 2 x AKG
Ligand 8T0 2 x 8T0
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: NSRRC BEAMLINE BL17A
Spacegroup: P62
Unit cell:
a: 171.361Å b: 171.361Å c: 45.559Å
α: 90° β: 90° γ: 120°
R-values:
R R work R free
0.21 0.207 0.255
Expression system: Escherichia coli

Quick links

Citations

4 review citations

Amazing Diversity in Biochemical Roles of Fe(II)/2-Oxoglutarate Oxygenases.
Herr et al. (2018)
3 more

2 mentions without citation

Structure function and engineering of multifunctional non-heme iron dependent oxygenases in fungal meroterpenoid biosynthesis.
Nakashima et al. (2018)
1 more