Structure of PDB 2qyo Chain B

Receptor sequence
>2qyoB (length=352) Species: 3880 (Medicago truncatula) [Search protein sequence]
NNRKPSEIFKAQALLYKNMYAFVDSMSLKWSIEMNIPNIIHNHGKPITLS
NLVSILQIPSTKVDNVQRLMRYLAHNGFFEIITNQELENEEEAYALTVAS
ELLVKGTELCLAPMVECVLDPTLSTSFHNLKKWVYEEDLTLFAVNLGCDL
WEFLNKNPEYNTLYNDALASDSKMINLAMKDCNLVFEGLESIVDVGGGNG
TTGKIICETFPKLTCVVFDRPKVVENLCGSNNLTYVGGDMFISVPKADAV
LLKAVLHDWTDKDCIKILKKCKEAVTSDGKRGKVIVIDMVINEKKDENQL
TQIKLLMNVTISCVNGKERNEEEWKKLFIEAGFQDYKISPFTGLMSLIEI
YP
3D structure
PDB2qyo Crystal structures of Medicago truncatula isoflavone O-methyltransferase reveal conserved surface binding motifs critical for enzymatic activity
ChainB
Resolution1.95 Å
3D
structure
Catalytic site residues are labeled in the structure
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Enzymatic activity
Catalytic site (original residue number in PDB) H262 D263 D293 E323
Catalytic site (residue number reindexed from 1) H257 D258 D288 E318
Enzyme Commision number 2.1.1.150: isoflavone 7-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 B G201 D224 R225 D244 M245 K258 G196 D219 R220 D239 M240 K253
BS02 QSO B V123 L128 S129 I316 V319 V118 L123 S124 I311 V314
Gene Ontology
Molecular Function
GO:0008168 methyltransferase activity
GO:0008171 O-methyltransferase activity
GO:0008757 S-adenosylmethionine-dependent methyltransferase activity
GO:0033800 isoflavone 7-O-methyltransferase activity
GO:0046983 protein dimerization activity
Biological Process
GO:0009058 biosynthetic process
GO:0032259 methylation

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Molecular Function
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Biological Process
External links
PDB RCSB:2qyo, PDBe:2qyo, PDBj:2qyo
PDBsum2qyo
PubMed
UniProtQ06YR3

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