Structure of PDB 5jr3 Chain B

Receptor sequence
>5jr3B (length=340) Species: 1950 (Streptomyces peucetius) [Search protein sequence]
QIDALRTLIRLGSLHTPMVVRTAATLRLVDHILAGARTVKALAARTDTRP
EALLRLIRHLVAIGLLEEDAPGEFVPTEVGELLADDHPAAQRAWHDLTQA
VARADISFTRLPDAIRTGRPTYESIYGKPFYEDLAGRPDLRASFDSLLAC
DQDVAFDAPAAAYDWTNVRHVLDVGGGKGGFAAAIARRAPHVSATVLEMA
GTVDTARSYLKDEGLSDRVDVVEGDFFEPLPRKADAIILSFVLLNWPDHD
AVRILTRCAEALEPGGRILIHERDDLHENSFNEQFTELDLRMLVFLGGAL
RTREKWDGLAASAGLVVEEVRQLPSPTIPYDLSLLVLAPA
3D structure
PDB5jr3 Crystal structure of carminomycin-4-O-methyltransferase DnrK in complex with SAH and 4-methylumbelliferone (to be published)
ChainB
Resolution1.84 Å
3D
structure
Catalytic site residues are labeled in the structure
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Enzymatic activity
Catalytic site (original residue number in PDB) L256 N257 E284 L312
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 Y143 R153 L160 G187 G188 E210 M211 G236 D237 F238 S252 F253 Y131 R141 L148 G175 G176 E198 M199 G224 D225 F226 S240 F241
BS02 4MU B L300 R303 L288 R291
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
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Biological Process
External links
PDB RCSB:5jr3, PDBe:5jr3, PDBj:5jr3
PDBsum5jr3
PubMed
UniProtQ06528|DNRK_STRPE Carminomycin 4-O-methyltransferase DnrK (Gene Name=dnrK)

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