Structure of PDB 3tky Chain B Binding Site BS02

Receptor Information
>3tky Chain B (length=349) Species: 36903 (Clarkia breweri) [Search protein sequence] [Download receptor structure] [Download structure with residue number starting from 1] [View receptor structure]
IQIIPTHSSDEEANLFAMQLASAAVLPMALKAAIELDVLEIMAKSVGYIS
PAEIAAQLPTTNPEAPVMLDRVLRLLASYSVVTYTLRERLYGLAPVCKFL
TKNEDGVSLAPFLLLATDKVLLEPWFYLKDAILEGGIPFNKAYGMNIFDY
HGTDHRINKVFNKGMSSNSTITMKKILEMYNGFEGLTTIVDVGGGTGAVA
SMIVAKYPSINAINFDLPHVIQDAPAFSGVEHLGGDMFDGVPKGDAIFIK
WICHDWSDEHCLKLLKNCYAALPDHGKVIVAEYILPPSPDPSIATKVVIH
TDALMLAYNPGGKERTEKEFQALAMASGFRGFKVASCAFNTYVMEFLKT
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 chain3tky Chain B Residue 370 [Download ligand structure] [Download structure with residue number starting from 1] [View ligand structure]
Receptor-Ligand Complex Structure
Global viewLocal viewStructure summary

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PDB3tky An engineered monolignol 4-o-methyltransferase depresses lignin biosynthesis and confers novel metabolic capability in Arabidopsis.
Resolution2.47 Å
Binding residue
(original residue number in PDB)		F166 S187 G211 G212 D234 L235 D254 M255 F256 K268 I270 W274
Binding residue
(residue number reindexed from 1)		F148 S169 G193 G194 D216 L217 D236 M237 F238 K250 I252 W256
Annotation score5
Enzymatic activity
Catalytic site (original residue number in PDB) H272 D273 E300 E332
Catalytic site (residue number reindexed from 1) H254 D255 E282 E314
Enzyme Commision number 2.1.1.146: (iso)eugenol O-methyltransferase.
Gene Ontology
Molecular Function
GO:0008168 methyltransferase activity
GO:0008171 O-methyltransferase activity
GO:0008757 S-adenosylmethionine-dependent methyltransferase activity
GO:0046983 protein dimerization activity
GO:0050630 (iso)eugenol O-methyltransferase activity
Biological Process
GO:0032259 methylation

View graph for
Molecular Function
View graph for
Biological Process
External links
PDB RCSB:3tky, PDBe:3tky, PDBj:3tky
PDBsum3tky
PubMed22851762
UniProtO04385|IEMT_CLABR (Iso)eugenol O-methyltransferase (Gene Name=IEMT1)

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