› 1xdu

X-ray diffraction
2.7Å resolution

Crystal structure of Aclacinomycin-10-hydroxylase (RdmB) in complex with Sinefungin (SFG)

Released:
DOI: 10.2210/pdb1xdu/pdb
PDB entry 1xdu coloured by chain, front view.
PDB entry 1xdu coloured by chain, side view.
PDB entry 1xdu coloured by chain, top view.
Source organism: Streptomyces purpurascens
Primary publication:
Aclacinomycin 10-hydroxylase is a novel substrate-assisted hydroxylase requiring S-adenosyl-L-methionine as cofactor.
Jansson A, Koskiniemi H, Erola A, Wang J, Mäntsälä P, Schneider G, Niemi J
J Biol Chem 280 3636-44 (2005)
PMID: 15548527

Function and Biology Details

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

Structure analysis Details

Assemblies composition:
monomeric (preferred)
homo dimer
Assembly name:
PDBe Complex ID:
PDB-CPX-176212 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Aclacinomycin 10-hydroxylase RdmB Chain: A
Molecule details ›
Chain: A
Length: 374 amino acids
Theoretical weight: 40.17 KDa
Source organism: Streptomyces purpurascens
Expression system: Escherichia coli
UniProt:
  • Canonical: Q54527 (Residues: 1-374; Coverage: 100%)
Gene name: rdmB
Sequence domains: O-methyltransferase domain
Structure domains:

Ligands and Environments

2 bound ligands:
Ligand ACT 1 x ACT
Ligand SFG 1 x SFG
1 modified residue:
Ligand MSE 7 x MSE

Experiments and Validation Details

Entry percentile scores
X-ray source: ESRF BEAMLINE ID29
Spacegroup: C2221
Unit cell:
a: 62.758Å b: 86.813Å c: 117.395Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.231 0.227 0.295
Expression system: Escherichia coli

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Citations

6 review citations

Flavoprotein monooxygenases, a diverse class of oxidative biocatalysts.
van Berkel et al. (2006)
5 more