Structure of PDB 3mwb Chain B Binding Site BS03

Receptor Information

>3mwb Chain B (length=303) Species: 290340 (Paenarthrobacter aurescens TC1)

VTYTFLGPQGTFTEAALMQVPGAADATRIPCTNVNTALERVRAGEADAAM
VPIENSVEGGVTATLDAIATGQELRIIREALVPITFVLVARPGVELSDIK
RISTHGHAWAQCRLWVDEHLPNADYVPGSSTAASAMGLLEDDAPYEAAIC
APLIAAEQPGLNVLAEDIGDNPDAVTRFILVSRPGALPERTGADKTTVVV
PLPEDHPGALMEILDQFASRGVNLSRIESRPTLGHYFFSIDADGHATDSR
VADALAGLHRISPATRFLGSYARADKQPAVVAPHTSDAAFASAHAWVDSI
LKG

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: 3mwb Chain B Residue 313

Receptor-Ligand Complex Structure

Structure summary

• PDB: 3mwb The Crystal Structure of Prephenate dehydratase in complex with L-Phe from Arthrobacter aurescens to 2.0A
• Resolution: 2.0 Å
• Binding residue (original residue number in PDB): A158 Q161 L164
• Binding residue (residue number reindexed from 1): A155 Q158 L161
• Annotation score: 1

Enzymatic activity

• Catalytic site (original residue number in PDB): T179 F181
• Catalytic site (residue number reindexed from 1): T176 F178
• Enzyme Commision number: 4.2.1.51: prephenate dehydratase.

Gene Ontology

Molecular Function

• GO:0004106 chorismate mutase activity
• GO:0004664 prephenate dehydratase activity
• GO:0016829 lyase activity
• GO:0016836 hydro-lyase activity
• GO:0046872 metal ion binding

Biological Process

• GO:0009094 L-phenylalanine biosynthetic process

Cellular Component

• GO:0005737 cytoplasm

External links

• PDB: RCSB:3mwb, PDBe:3mwb, PDBj:3mwb
• PDBsum: 3mwb
• UniProt: A1R118