Structure of PDB 1tw3 Chain A

Receptor sequence

>1tw3A (length=340) Species: 1950 (Streptomyces peucetius)

QIDALRTLIRLGSLHTPMVVRTAATLRLVDHILAGARTVKALAARTDTRP
EALLRLIRHLVAIGLLEEDAPGEFVPTEVGELLADDHPAAQRAWHDLTQA
VARADISFTRLPDAIRTGRPTYESIYGKPFYEDLAGRPDLRASFDSLLAC
DQDVAFDAPAAAYDWTNVRHVLDVGGGKGGFAAAIARRAPHVSATVLEMA
GTVDTARSYLKDEGLSDRVDVVEGDFFEPLPRKADAIILSFVLLNWPDHD
AVRILTRCAEALEPGGRILIHERDDLHENSFNEQFTELDLRMLVFLGGAL
RTREKWDGLAASAGLVVEEVRQLPSPTIPYDLSLLVLAPA

3D structure

• PDB: 1tw3 Crystal structure of a ternary complex of DnrK, a methyltransferase in daunorubicin biosynthesis, with bound products
• Chain: A
• Resolution: 2.35 Å

Enzymatic activity

• Catalytic site (original residue number in PDB): L255 N256 E283 L311
• Catalytic site (residue number reindexed from 1): L244 N245 E272 L300
• Enzyme Commision number: 2.1.1.292: carminomycin 4-O-methyltransferase.

Interaction with ligand

Site #	Ligand	Ligand chain	Binding residues on receptor (original residue number in PDB)	Binding residues on receptor (residue number reindexed from 1)	Binding affinity
BS01	SAH	A	Y142 R152 L159 F167 G186 G187 E209 M210 G235 D236 F237 S251 F252	Y131 R141 L148 F156 G175 G176 E198 M199 G224 D225 F226 S240 F241
BS02	ERT	A	W105 F155 L159 D162 F252 N256 E298 L299 R302 F306	W94 F144 L148 D151 F241 N245 E287 L288 R291 F295

Gene Ontology

Molecular Function

• GO:0008168 methyltransferase activity
• GO:0008171 O-methyltransferase activity

Biological Process

• GO:0017000 antibiotic biosynthetic process
• GO:0032259 methylation
• GO:1901771 daunorubicin biosynthetic process

External links

• PDB: RCSB:1tw3, PDBe:1tw3, PDBj:1tw3
• PDBsum: 1tw3
• PubMed: 15273252
• UniProt: Q06528|DNRK_STRPE Carminomycin 4-O-methyltransferase DnrK (Gene Name=dnrK)