Structure of PDB 4pio Chain B

Receptor sequence
>4pioB (length=318) Species: 1772 (Mycolicibacterium smegmatis) [Search protein sequence]
SLANYLAADSAAEALRRDVRAGLTATQKSLPPKWFYDAVGSDLFDQITRL
PEYYPTRTEAQILRTRSAEIISAAGADTLVELGSGTSEKTRMLLDAMRDA
ELLRRFIPFDVDAGVLRSAGAAIGAEYPGIEIDAVCGDFEEHLGKIPHVG
RRLVVFLGSTIGNLTPAPRAEFLSTLADTLQPGDSLLLGTDLVKDTGRLV
RAYDDAAGVTAAFNRNVLAVVNRELSADFDLDAFEHVAKWNSDEERIEMW
LRARTAQHVRVAALDLEVDFAAGEEMLTEVSDKFRPENVVAELAEAGLRQ
THWWTDPAGDFGLSLAVR
3D structure
PDB4pio Ergothioneine Biosynthetic Methyltransferase EgtD Reveals the Structural Basis of Aromatic Amino Acid Betaine Biosynthesis.
ChainB
Resolution1.506 Å
3D
structure
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Enzymatic activity
Enzyme Commision number 2.1.1.44: L-histidine N(alpha)-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 Y39 F47 G86 G88 K92 D113 V114 G140 D141 F142 Y36 F44 G83 G85 K89 D110 V111 G137 D138 F139 MOAD: Kd=210uM
BS02 AVI B Y56 G161 S162 T163 N166 Y206 E282 S284 Y53 G158 S159 T160 N163 Y203 E279 S281 MOAD: Kd=2uM
Gene Ontology
Molecular Function
GO:0008168 methyltransferase activity
GO:0008276 protein methyltransferase activity
GO:0052706 L-histidine N(alpha)-methyltransferase activity
Biological Process
GO:0032259 methylation
GO:0052699 ergothioneine biosynthetic process
GO:0052704 ergothioneine biosynthesis from histidine via gamma-glutamyl-hercynylcysteine sulfoxide

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Molecular Function
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Biological Process
External links
PDB RCSB:4pio, PDBe:4pio, PDBj:4pio
PDBsum4pio
PubMed25404173
UniProtA0R5M8|EGTD_MYCS2 Histidine N-alpha-methyltransferase (Gene Name=egtD)

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