Structure of PDB 1zgj Chain A

Receptor sequence
>1zgjA (length=354) Species: 3880 (Medicago truncatula) [Search protein sequence]
SELYHAQIHLYKHVYNFVSSMALKSAMELGIADAIHNHGKPMTLSELASS
LKLHPSKVNILHRFLRLLTHNGFFAKTIVKGKEGDEEEEIAYSLTPPSKL
LISGKPTCLSSIVKGALHPSSLDMWSSSKKWFNEDKEQTLFECATGESFW
DFLNKDSESSTLSMFQDAMASDSRMFKLVLQENKRVFEGLESLVDVGGGT
GGVTKLIHEIFPHLKCTVFDQPQVVGNLTGNENLNFVGGDMFKSIPSADA
VLLKWVLHDWNDEQSLKILKNSKEAISHKGKDGKVIIIDISIDETSDDRG
LTELQLDYDLVMLTMFLGKERTKQEWEKLIYDAGFSSYKITPISGFKSLI
EVYP
3D structure
PDB1zgj 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) H258 D259 D289 E320
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 P1S A G125 A126 S131 F159 M174 F175 M179 Y318 M322 G115 A116 S121 F149 M164 F165 M169 Y308 M312
BS02 SAH A G207 V213 D230 Q231 D250 M251 F252 K264 G197 V203 D220 Q221 D240 M241 F242 K254
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

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Molecular Function

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Biological Process
External links
PDB RCSB:1zgj, PDBe:1zgj, PDBj:1zgj
PDBsum1zgj
PubMed17172354
UniProtQ29U70|I4OMT_MEDTR Isoflavone 4'-O-methyltransferase (Gene Name=HI4'OMT)

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