› 6c3b

X-ray diffraction
1.51Å resolution

O2-, PLP-Dependent L-Arginine Hydroxylase RohP Holoenzyme

Released:
DOI: 10.2210/pdb6c3b/pdb
PDB entry 6c3b coloured by chain, front view.
PDB entry 6c3b coloured by chain, side view.
PDB entry 6c3b coloured by chain, top view.
Source organism: Streptomyces cattleya NRRL 8057 = DSM 46488
Primary publication:
Snapshots of the Catalytic Cycle of an O2, Pyridoxal Phosphate-Dependent Hydroxylase.
Hedges JB, Kuatsjah E, Du YL, Eltis LD, Ryan KS
ACS Chem Biol 13 965-974 (2018)
PMID: 29466666

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-124645 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Aminotransferase class I/classII domain-containing protein Chains: A, B
Molecule details ›
Chains: A, B
Length: 413 amino acids
Theoretical weight: 47.51 KDa
Source organism: Streptomyces cattleya NRRL 8057 = DSM 46488
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: G8WNK6 (Residues: 1-368; Coverage: 100%)
Gene name: SCATT_03970
Sequence domains: Aminotransferase class I and II

Ligands and Environments

2 bound ligands:
Ligand EDO 14 x EDO
Ligand PGE 3 x PGE
1 modified residue:
Ligand LLP 2 x LLP

Experiments and Validation Details

Entry percentile scores
X-ray source: CLSI BEAMLINE 08ID-1
Spacegroup: C2
Unit cell:
a: 79.38Å b: 112.41Å c: 102.16Å
α: 90° β: 95.77° γ: 90°
R-values:
R R work R free
0.153 0.152 0.172
Expression system: Escherichia coli BL21(DE3)

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Citations

2 review citations

Pyridoxal phosphate-dependent reactions in the biosynthesis of natural products.
Du et al. (2019)
1 more

1 mention without citation

A shared mechanistic pathway for pyridoxal phosphate-dependent arginine oxidases.
Hoffarth et al. (2021)