Structure of PDB 4pip Chain D

Receptor sequence
>4pipD (length=318) Species: 1772 (Mycolicibacterium smegmatis) [Search protein sequence]
SLANYLAADSAAEALRRDVRAGLTATQKSLPPKWFYDAVGSDLFDQITRL
PEYYPTRTEAQILRTRSAEIISAAGADTLVELGSGTSEKTRMLLDAMRDA
ELLRRFIPFDVDAGVLRSAGAAIGAEYPGIEIDAVCGDFEEHLGKIPHVG
RRLVVFLGSTIGNLTPAPRAEFLSTLADTLQPGDSLLLGTDLVKDTGRLV
RAYDDAAGVTAAFNRNVLAVVNRELSADFDLDAFEHVAKWNSDEERIEVW
LRARTAQHVRVAALDLEVDFAAGEEMLTAVSCKFRPENVVAELAEAGLRQ
THWWTDPAGDFGLSLAVR
3D structure
PDB4pip Ergothioneine Biosynthetic Methyltransferase EgtD Reveals the Structural Basis of Aromatic Amino Acid Betaine Biosynthesis.
ChainD
Resolution1.8 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 TRP D F47 Y56 N166 Y206 F216 S284 F44 Y53 N163 Y203 F213 S281
BS02 SAH D Y39 F47 G86 S87 G88 K92 D113 V114 G140 D141 F142 Y36 F44 G83 S84 G85 K89 D110 V111 G137 D138 F139
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:4pip, PDBe:4pip, PDBj:4pip
PDBsum4pip
PubMed25404173
UniProtA0R5M8|EGTD_MYCS2 Histidine N-alpha-methyltransferase (Gene Name=egtD)

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