Structure of PDB 1tw2 Chain B Binding Site BS01

Receptor Information
>1tw2 Chain B (length=350) Species: 1950 (Streptomyces peucetius) [Search protein sequence] [Download receptor structure] [Download structure with residue number starting from 1] [View receptor structure]
EPTVAARPQQIDALRTLIRLGSLHTPMVVRTAATLRLVDHILAGARTVKA
LAARTDTRPEALLRLIRHLVAIGLLEEDAPGEFVPTEVGELLADDHPAAQ
RAWHDLTQAVARADISFTRLPDAIRTGRPTYESIYGKPFYEDLAGRPDLR
ASFDSLLACDQDVAFDAPAAAYDWTNVRHVLDVGGGKGGFAAAIARRAPH
VSATVLEMAGTVDTARSYLKDEGLSDRVDVVEGDFFEPLPRKADAIILSF
VLLNWPDHDAVRILTRCAEALEPGGRILIHERDDLHENSFNEQFTELDLR
MLVFLGGALRTREKWDGLAASAGLVVEEVRQLPSPTIPYDLSLLVLAPAA
Ligand information
Ligand IDSAH
InChIInChI=1S/C14H20N6O5S/c15-6(14(23)24)1-2-26-3-7-9(21)10(22)13(25-7)20-5-19-8-11(16)17-4-18-12(8)20/h4-7,9-10,13,21-22H,1-3,15H2,(H,23,24)(H2,16,17,18)/t6-,7+,9+,10+,13+/m0/s1
InChIKeyZJUKTBDSGOFHSH-WFMPWKQPSA-N
SMILES
SoftwareSMILES
CACTVS 3.341N[CH](CCSC[CH]1O[CH]([CH](O)[CH]1O)n2cnc3c(N)ncnc23)C(O)=O
OpenEye OEToolkits 1.5.0c1nc(c2c(n1)n(cn2)C3C(C(C(O3)CSCCC(C(=O)O)N)O)O)N
CACTVS 3.341N[C@@H](CCSC[C@H]1O[C@H]([C@H](O)[C@@H]1O)n2cnc3c(N)ncnc23)C(O)=O
ACDLabs 10.04O=C(O)C(N)CCSCC3OC(n2cnc1c(ncnc12)N)C(O)C3O
OpenEye OEToolkits 1.5.0c1nc(c2c(n1)n(cn2)[C@H]3[C@@H]([C@@H]([C@H](O3)CSCC[C@@H](C(=O)O)N)O)O)N
FormulaC14 H20 N6 O5 S
NameS-ADENOSYL-L-HOMOCYSTEINE
ChEMBLCHEMBL418052
DrugBankDB01752
ZINCZINC000004228232
PDB chain1tw2 Chain B Residue 1635 [Download ligand structure] [Download structure with residue number starting from 1] [View ligand structure]
Receptor-Ligand Complex Structure
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PDB1tw2 Crystal structure of a ternary complex of DnrK, a methyltransferase in daunorubicin biosynthesis, with bound products
Resolution2.5 Å
Binding residue
(original residue number in PDB)		Y142 R152 L159 F167 G186 G187 E209 M210 G235 D236 F237 S251 F252
Binding residue
(residue number reindexed from 1)		Y140 R150 L157 F165 G184 G185 E207 M208 G233 D234 F235 S249 F250
Annotation score5
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.
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

View graph for
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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