Structure of PDB 3b5i Chain A

Receptor sequence
>3b5iA (length=344) Species: 3702 (Arabidopsis thaliana) [Search protein sequence]
AMHARSMLHLLEETLENVHLNSSASPPPFTAVDLGCSSGANTVHIIDFIV
KHISKRFDAAGIDPPEFTAFFSDLPSNDFNTLFQLLPPLVSNTEECDGNR
SYFVAGVPGSFYRRLFPARTIDFFHSAFSLHWLSQVPESVTDRRSAAYNR
GRVFIHGAGEKTTTAYKRQFQADLAEFLRARAAEVKRGGAMFLVCLGRTS
VDPTDQGGAGLLFGTHFQDAWDDLVREGLVAAEKRDGFNIPVYAPSLQDF
KEVVDANGSFAIDKLVVYKGGSPLVVNEPDDASEVGRAFASSCRSVAGVL
VEAHIGEELSNKLFSRVESRATSHAKDVLVNLQFFHIVASLSFT
3D structure
PDB3b5i Structural, Biochemical, and Phylogenetic Analyses Suggest That Indole-3-Acetic Acid Methyltransferase Is an Evolutionarily Ancient Member of the SABATH Family.
ChainA
Resolution2.75 Å
3D
structure
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Enzymatic activity
Enzyme Commision number 2.1.1.278: indole-3-acetate 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 G60 N66 D98 L99 S140 F141 Y142 A157 F158 S159 G35 N41 D73 L74 S110 F111 Y112 A127 F128 S129
BS02 MG A V183 R265 D266 F268 N269 V153 R235 D236 F238 N239
Gene Ontology
Molecular Function
GO:0000287 magnesium ion binding
GO:0008168 methyltransferase activity
GO:0042802 identical protein binding
GO:0046872 metal ion binding
GO:0051749 indole acetic acid carboxyl methyltransferase activity
GO:0103007 indole-3-acetate carboxyl methyltransferase activity
Biological Process
GO:0009851 auxin biosynthetic process
GO:0009944 polarity specification of adaxial/abaxial axis
GO:0032259 methylation
Cellular Component
GO:0005575 cellular_component

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Molecular Function
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Biological Process
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Cellular Component
External links
PDB RCSB:3b5i, PDBe:3b5i, PDBj:3b5i
PDBsum3b5i
PubMed18162595
UniProtQ9FLN8|IAMT1_ARATH Indole-3-acetate O-methyltransferase 1 (Gene Name=IAMT1)

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