Structure of PDB 4ymh Chain A

Receptor sequence
>4ymhA (length=239) [Search protein sequence]
LGSILPFNEETADRVSAYCEKNSHGIPDALVEHWEWTRTRFPDADKMSSR
LQGSWMIFTARDRKPKRILEIGCYSGYSALAWYEGTRDTKAEIVTLEYSP
KMIAASREAFKKYGVGDRVKLIEGPAENTLKTLEGEFDLIFVDANKDGYA
GYVKTILDQGLLSANGIILCDNVFARGLTIGPDCAPWLNDHVRPYWNGCG
QALDKFSAGLMEDPRIDVLLLPVFDGVTQIRWKDGAQRA
3D structure
PDB4ymh Structure and Biophysical Characterization of the S-Adenosylmethionine-dependent O-Methyltransferase PaMTH1, a Putative Enzyme Accumulating during Senescence of Podospora anserina.
ChainA
Resolution1.876 Å
3D
structure
Catalytic site residues are labeled in the structure
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Enzymatic activity
Catalytic site (original residue number in PDB) D144 K147 D172 N173
Catalytic site (residue number reindexed from 1) D143 K146 D171 N172
Enzyme Commision number ?
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 K47 M48 S49 G73 Y75 S79 E98 Y99 A127 D144 N146 K46 M47 S48 G72 Y74 S78 E97 Y98 A126 D143 N145 MOAD: Kd=3.2uM
PDBbind-CN: -logKd/Ki=6.46,Kd=0.35uM
Gene Ontology
Molecular Function
GO:0008168 methyltransferase activity
GO:0008171 O-methyltransferase activity
GO:0008757 S-adenosylmethionine-dependent methyltransferase activity
Biological Process
GO:0032259 methylation

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Molecular Function
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Biological Process
External links
PDB RCSB:4ymh, PDBe:4ymh, PDBj:4ymh
PDBsum4ymh
PubMed25979334
UniProtQ9HGR1

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