Structure of PDB 1zhf Chain A

Receptor sequence
>1zhfA (length=357) Species: 3880 (Medicago truncatula) [Search protein sequence]
SEESELYHAQIHLYKHVYNFVSSMALKSAMELGIADAIHNHGKPMTLSEL
ASSLKLHPSKVNILHRFLRLLTHNGFFAKTIVKGKEGDEEEEIAYSLTPP
SKLLISGKPTCLSSIVKGALHPSSLDMWSSSKKWFNEDKEQTLFECATGE
SFWDFLNKDSESSTLSMFQDAMASDSRMFKLVLQENKRVFEGLESLVDVG
GGTGGVTKLIHEIFPHLKCTVFDQPQVVGNLTGNENLNFVGGDMFKSIPS
ADAVLLKWVLHDWNDEQSLKILKNSKEAISHKGKDGKVIIIDISIDETSD
DRGLTELQLDYDLVMLTMFLGKERTKQEWEKLIYDAGFSSYKITPISGFK
SLIEVYP
3D structure
PDB1zhf Structural basis for dual functionality of isoflavonoid O-methyltransferases in the evolution of plant defense responses.
ChainA
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) H268 D269 D299 E330
Catalytic site (residue number reindexed from 1) H261 D262 D292 E323
Enzyme Commision number 2.1.1.212: 2,7,4'-trihydroxyisoflavanone 4'-O-methyltransferase.
2.1.1.46: isoflavone 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 A G207 D230 Q231 D250 M251 K264 G200 D223 Q224 D243 M244 K257
Gene Ontology
Molecular Function
GO:0008168 methyltransferase activity
GO:0008171 O-methyltransferase activity
GO:0008757 S-adenosylmethionine-dependent methyltransferase activity
GO:0030746 isoflavone 4'-O-methyltransferase activity
GO:0046983 protein dimerization activity
GO:0102670 2,7,4'-trihydroxyisoflavanone-4'-O-methyltransferase activity
Biological Process
GO:0032259 methylation

View graph for
Molecular Function

View graph for
Biological Process
External links
PDB RCSB:1zhf, PDBe:1zhf, PDBj:1zhf
PDBsum1zhf
PubMed17172354
UniProtQ29U70|I4OMT_MEDTR Isoflavone 4'-O-methyltransferase (Gene Name=HI4'OMT)

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