Structure of PDB 1fpq Chain A Binding Site BS01

Receptor Information
>1fpq Chain A (length=333) Species: 3879 (Medicago sativa) [Search protein sequence] [Download receptor structure] [Download structure with residue number starting from 1] [View receptor structure]
TEDSACLSAMVLTTNLVYPAVLNAAIDLNLFEIIAKATPPGAFMSPSEIA
SKLPASTQHSDLPNRLDRMLRLLASYSVLTSTTRTIEDGGAERVYGLSMV
GKYLVPDESRGYLASFTTFLCYPALLQVWMNFKEAVVDEDKMNQIFNKSM
VDVCATEMKRMLEIYTGFEGISTLVDVGGGSGRNLELIISKYPLIKGINF
DLPQVIENAPPLSGIEHVGGDMFASVPQGDAMILKAVCHNWSDEKCIEFL
SNCHKALSPNGKVIIVEFILPEEPNTSEESKLVSTLDNLMFITVGGRERT
EKQYEKLSKLSGFSKFQVACRAFNSLGVMEFYK
Ligand information
Ligand IDSAM
InChIInChI=1S/C15H22N6O5S/c1-27(3-2-7(16)15(24)25)4-8-10(22)11(23)14(26-8)21-6-20-9-12(17)18-5-19-13(9)21/h5-8,10-11,14,22-23H,2-4,16H2,1H3,(H2-,17,18,19,24,25)/t7-,8+,10+,11+,14+,27-/m0/s1
InChIKeyMEFKEPWMEQBLKI-FCKMPRQPSA-N
SMILES
SoftwareSMILES
CACTVS 3.341C[S@@+](CC[C@H](N)C([O-])=O)C[C@H]1O[C@H]([C@H](O)[C@@H]1O)n2cnc3c(N)ncnc23
OpenEye OEToolkits 1.5.0C[S+](CCC(C(=O)[O-])N)CC1C(C(C(O1)n2cnc3c2ncnc3N)O)O
CACTVS 3.341C[S+](CC[CH](N)C([O-])=O)C[CH]1O[CH]([CH](O)[CH]1O)n2cnc3c(N)ncnc23
OpenEye OEToolkits 1.5.0C[S@@+](CC[C@@H](C(=O)[O-])N)C[C@@H]1[C@H]([C@H]([C@@H](O1)n2cnc3c2ncnc3N)O)O
ACDLabs 10.04[O-]C(=O)C(N)CC[S+](C)CC3OC(n2cnc1c(ncnc12)N)C(O)C3O
FormulaC15 H22 N6 O5 S
NameS-ADENOSYLMETHIONINE
ChEMBLCHEMBL1235831
DrugBank
ZINC
PDB chain1fpq Chain A Residue 1699 [Download ligand structure] [Download structure with residue number starting from 1] [View ligand structure]
Receptor-Ligand Complex Structure
Global viewLocal viewStructure summary

[Spin on] [Spin off] [Reset]
[High quality] [Low quality]
[White background] [Black background]
[Spin on] [Spin off] [Reset]
[High quality] [Low quality]
[White background] [Black background]
PDB1fpq Structures of two natural product methyltransferases reveal the basis for substrate specificity in plant O-methyltransferases.
Resolution2.0 Å
Binding residue
(original residue number in PDB)		G217 D240 L241 D260 M261 F262 K274 A275
Binding residue
(residue number reindexed from 1)		G178 D201 L202 D221 M222 F223 K235 A236
Annotation score5
Enzymatic activity
Catalytic site (original residue number in PDB) H278 N279 E306 E337
Catalytic site (residue number reindexed from 1) H239 N240 E267 E298
Enzyme Commision number 2.1.1.154: isoliquiritigenin 2'-O-methyltransferase.
2.1.1.65: licodione 2'-O-methyltransferase.
Gene Ontology
Molecular Function
GO:0008168 methyltransferase activity
GO:0008171 O-methyltransferase activity
GO:0008757 S-adenosylmethionine-dependent methyltransferase activity
GO:0030751 licodione 2'-O-methyltransferase activity
GO:0033802 isoliquiritigenin 2'-O-methyltransferase activity
GO:0046983 protein dimerization activity
Biological Process
GO:0032259 methylation

View graph for
Molecular Function
View graph for
Biological Process
External links
PDB RCSB:1fpq, PDBe:1fpq, PDBj:1fpq
PDBsum1fpq
PubMed11224575
UniProtP93324|CHOMT_MEDSA Isoliquiritigenin 2'-O-methyltransferase

[Back to BioLiP]