› 7phe

X-ray diffraction
2.32Å resolution

Chimeric carminomycin-4-O-methyltransferase (DnrK) with regions from 10-hydroxylase RdmB and 10-decarboxylase TamK

Released:
DOI: 10.2210/pdb7phe/pdb
PDB entry 7phe coloured by chain, front view.
PDB entry 7phe coloured by chain, side view.
PDB entry 7phe coloured by chain, top view.
Source organisms:
Primary publication:
Evolution-inspired engineering of anthracycline methyltransferases.
Dinis P, Tirkkonen H, Wandi BN, Siitonen V, Niemi J, Grocholski T, Metsä-Ketelä M
OpenAccess logo PNAS Nexus 2 pgad009 (2023)
PMID: 36874276

Function and Biology Details

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

Structure analysis Details

Assembly composition:
homo dimer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-125061 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Aclacinomycin 10-hydroxylase RdmB; Carminomycin 4-O-methyltransferase DnrK; O-methyltransferase domain-containing protein Chains: A, B
Molecule details ›
Chains: A, B
Length: 368 amino acids
Theoretical weight: 39.98 KDa
Source organisms: Expression system: Escherichia coli
UniProt:
  • Canonical: Q06528 (Residues: 2-159, 172-188, 193-285, 311-333, 347-356; Coverage: 85%)
  • Canonical: I2N5E8 (Residues: 169-180, 198-201, 295-295, 318-322, 346-359; Coverage: 10%)
  • Canonical: Q54527 (Residues: 290-309; Coverage: 5%)
Gene names: STSU_011780, dnrK, rdmB
Sequence domains: O-methyltransferase domain

Ligands and Environments

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

Experiments and Validation Details

Entry percentile scores
X-ray source: MAX IV BEAMLINE BioMAX
Spacegroup: P21
Unit cell:
a: 58.8Å b: 110.4Å c: 64.21Å
α: 90° β: 108.648° γ: 90°
R-values:
R R work R free
0.215 0.213 0.255
Expression system: Escherichia coli

Quick links