Chimeric carminomycin-4-O-methyltransferase (dnrk) with regions from 10-decarboxylate tamk and 10-hydroxylase rdmb, together with a single point mutation F297G

Structure

x-ray diffraction · 1 distinct chain · 47% helix, 16% strand (DSSP).

Ligands and binding sites

• SAH · S-adenosyl-L-homocysteine · ligand · chains A
• ZBX · methyl (1R,2R,4S)-2-ethyl-7-methoxy-2,4,5-tris(oxidanyl)-6,11-bis(oxidanylidene)-3,4-dihydro-1H-tetracene-1-carboxylate · ligand · chains A

Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.

Pockets

2 pockets found on a 1 Å grid, 1 with a druggability of 0.5 or more.

Compared structures

• 7PGJ · Chimeric carminomycin-4-O-methyltransferase (DnrK) with regions from 10-decarboxylate… · the same entry in another collection · chain A against A, TM-score 1.00
• Q06528 · AlphaFold monomer V2.0 prediction for carminomycin 4-O-methyltransferase dnrk (Q06528) · a predicted model of the same protein · chain A against A, TM-score 0.97
• Q54527 · AlphaFold monomer V2.0 prediction for aclacinomycin 10-hydroxylase rdmb (Q54527) · a predicted model of the same protein · chain A against A, TM-score 0.94

Analyse

• Open in the research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides and crosslinks on the 3D structure
• Every structure of UniProt Q06528
• Every structure of UniProt I2N5E8
• Every structure of UniProt Q54527
• Elsewhere: RCSB PDB 7PGJ · PDBe 7PGJ · UniProt Q06528 · UniProt I2N5E8 · UniProt Q54527