Structure of PDB 1tw3 Chain B

Receptor sequence
>1tw3B (length=340) Species: 1950 (Streptomyces peucetius) [Search protein sequence]
QIDALRTLIRLGSLHTPMVVRTAATLRLVDHILAGARTVKALAARTDTRP
EALLRLIRHLVAIGLLEEDAPGEFVPTEVGELLADDHPAAQRAWHDLTQA
VARADISFTRLPDAIRTGRPTYESIYGKPFYEDLAGRPDLRASFDSLLAC
DQDVAFDAPAAAYDWTNVRHVLDVGGGKGGFAAAIARRAPHVSATVLEMA
GTVDTARSYLKDEGLSDRVDVVEGDFFEPLPRKADAIILSFVLLNWPDHD
AVRILTRCAEALEPGGRILIHERDDLHENSFNEQFTELDLRMLVFLGGAL
RTREKWDGLAASAGLVVEEVRQLPSPTIPYDLSLLVLAPA
3D structure
PDB1tw3 Crystal structure of a ternary complex of DnrK, a methyltransferase in daunorubicin biosynthesis, with bound products
ChainB
Resolution2.35 Å
3D
structure
Catalytic site residues are labeled in the structure
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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 B Y142 R152 F167 G186 E209 M210 G235 D236 F237 S251 F252 Y131 R141 F156 G175 E198 M199 G224 D225 F226 S240 F241
BS02 ERT B 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

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Molecular Function
View graph for
Biological Process
External links
PDB RCSB:1tw3, PDBe:1tw3, PDBj:1tw3
PDBsum1tw3
PubMed15273252
UniProtQ06528|DNRK_STRPE Carminomycin 4-O-methyltransferase DnrK (Gene Name=dnrK)

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