Structure of PDB 1tw2 Chain B

Receptor sequence
>1tw2B (length=350) Species: 1950 (Streptomyces peucetius) [Search protein sequence]
EPTVAARPQQIDALRTLIRLGSLHTPMVVRTAATLRLVDHILAGARTVKA
LAARTDTRPEALLRLIRHLVAIGLLEEDAPGEFVPTEVGELLADDHPAAQ
RAWHDLTQAVARADISFTRLPDAIRTGRPTYESIYGKPFYEDLAGRPDLR
ASFDSLLACDQDVAFDAPAAAYDWTNVRHVLDVGGGKGGFAAAIARRAPH
VSATVLEMAGTVDTARSYLKDEGLSDRVDVVEGDFFEPLPRKADAIILSF
VLLNWPDHDAVRILTRCAEALEPGGRILIHERDDLHENSFNEQFTELDLR
MLVFLGGALRTREKWDGLAASAGLVVEEVRQLPSPTIPYDLSLLVLAPAA
3D structure
PDB1tw2 Crystal structure of a ternary complex of DnrK, a methyltransferase in daunorubicin biosynthesis, with bound products
ChainB
Resolution2.5 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) L253 N254 E281 L309
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 L159 F167 G186 G187 E209 M210 G235 D236 F237 S251 F252 Y140 R150 L157 F165 G184 G185 E207 M208 G233 D234 F235 S249 F250
BS02 ERT B W105 F155 L159 F252 N256 L299 R302 W103 F153 L157 F250 N254 L297 R300
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:1tw2, PDBe:1tw2, PDBj:1tw2
PDBsum1tw2
PubMed15273252
UniProtQ06528|DNRK_STRPE Carminomycin 4-O-methyltransferase DnrK (Gene Name=dnrK)

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