Structure of PDB 4pip Chain C

Receptor sequence
>4pipC (length=315) Species: 1772 (Mycolicibacterium smegmatis) [Search protein sequence]
GHMALSLAAEALRRDVRAGLTATQKSLPPKWFYDAVGSDLFDQITRLPEY
YPTRTEAQILRTRSAEIISAAGADTLVELGSGTSEKTRMLLDAMRDAELL
RRFIPFDVDAGVLRSAGAAIGAEYPGIEIDAVCGDFEEHLGKIPHVGRRL
VVFLGSTIGNLTPAPRAEFLSTLADTLQPGDSLLLGTDLVKDTGRLVRAY
DDAAGVTAAFNRNVLAVVNRELSADFDLDAFEHVAKWNSDEERIEVWLRA
RTAQHVRVAALDLEVDFAAGEEMLTAVSCKFRPENVVAELAEAGLRQTHW
WTDPAGDFGLSLAVR
3D structure
PDB4pip Ergothioneine Biosynthetic Methyltransferase EgtD Reveals the Structural Basis of Aromatic Amino Acid Betaine Biosynthesis.
ChainC
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 C F47 Y56 N166 Y206 F216 S284 F41 Y50 N160 Y200 F210 S278
BS02 SAH C Y39 F47 G86 G88 K92 D113 V114 G140 D141 F142 T163 Y33 F41 G80 G82 K86 D107 V108 G134 D135 F136 T157
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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