Structure of PDB 4pio Chain A Binding Site BS03

Receptor Information

>4pio Chain A (length=307) Species: 1772 (Mycolicibacterium smegmatis)

AEALRRDVRAGLTATQKSLPPKWFYDAVGSDLFDQITRLPEYYPTRTEAQ
ILRTRSAEIISAAGADTLVELGSGTSEKTRMLLDAMRDAELLRRFIPFDV
DAGVLRSAGAAIGAEYPGIEIDAVCGDFEEHLGKIPHVGRRLVVFLGSTI
GNLTPAPRAEFLSTLADTLQPGDSLLLGTDLVKDTGRLVRAYDDAAGVTA
AFNRNVLAVVNRELSADFDLDAFEHVAKWNSDEERIEMWLRARTAQHVRV
AALDLEVDFAAGEEMLTEVSDKFRPENVVAELAEAGLRQTHWWTDPAGDF
GLSLAVR

Ligand information

• Ligand ID: MG
• InChI: InChI=1S/Mg/q+2
• InChIKey: JLVVSXFLKOJNIY-UHFFFAOYSA-N
• SMILES:
  ACDLabs 10.04
  OpenEye OEToolkits 1.5.0: [Mg+2]
  CACTVS 3.341: [Mg++]
• Formula: Mg
• Name: MAGNESIUM ION
• DrugBank: DB01378
• PDB chain: 4pio Chain A Residue 405

Receptor-Ligand Complex Structure

Structure summary

• PDB: 4pio Ergothioneine Biosynthetic Methyltransferase EgtD Reveals the Structural Basis of Aromatic Amino Acid Betaine Biosynthesis.
• Resolution: 1.506 Å
• Binding residue (original residue number in PDB): D233 D235
• Binding residue (residue number reindexed from 1): D219 D221
• Annotation score: 1

Enzymatic activity

• Enzyme Commision number: 2.1.1.44: L-histidine N(alpha)-methyltransferase.

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

External links

• PDB: RCSB:4pio, PDBe:4pio, PDBj:4pio
• PDBsum: 4pio
• PubMed: 25404173
• UniProt: A0R5M8|EGTD_MYCS2 Histidine N-alpha-methyltransferase (Gene Name=egtD)