› 5eeg

X-ray diffraction
2.26Å resolution

Crystal structure of carminomycin-4-O-methyltransferase DnrK in complex with tetrazole-SAH

Released:
DOI: 10.2210/pdb5eeg/pdb
PDB entry 5eeg coloured by chain, front view.
PDB entry 5eeg coloured by chain, side view.
PDB entry 5eeg coloured by chain, top view.
Source organism: Streptomyces peucetius
Primary publication:
Functional AdoMet Isosteres Resistant to Classical AdoMet Degradation Pathways.
Huber TD, Wang F, Singh S, Johnson BR, Zhang J, Sunkara M, Van Lanen SG, Morris AJ, Phillips GN, Thorson JS
ACS Chem Biol 11 2484-91 (2016)
PMID: 27351335

Function and Biology Details

Reaction catalysed: 
S-adenosyl-L-methionine + carminomycin = S-adenosyl-L-homocysteine + daunorubicin
Biochemical function:
Biological process:
Cellular component:
  • not assigned
Sequence domains:

Structure analysis Details

Assembly composition:
homo dimer (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Carminomycin 4-O-methyltransferase DnrK Chains: A, B
Molecule details ›
Chains: A, B
Length: 376 amino acids
Theoretical weight: 41 KDa
Source organism: Streptomyces peucetius
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: Q06528 (Residues: 1-356; Coverage: 100%)
Gene name: dnrK
Sequence domains: O-methyltransferase domain
Structure domains:

Ligands and Environments

1 bound ligand:
Ligand S8M 2 x S8M
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: APS BEAMLINE 21-ID-F
Spacegroup: P21
Unit cell:
a: 60.562Å b: 104.18Å c: 62.986Å
α: 90° β: 105.2° γ: 90°
R-values:
R R work R free
0.2 0.197 0.248
Expression system: Escherichia coli BL21(DE3)

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Citations

5 review citations

Enzymatic Late-Stage Modifications: Better Late Than Never.
Romero et al. (2021)
4 more

1 mention without citation

Mechanisms of protein evolution.
Jayaraman et al. (2022)