Structure of PDB 3mwb Chain A

Receptor sequence
>3mwbA (length=306) Species: 290340 (Paenarthrobacter aurescens TC1) [Search protein sequence]
VTYTFLGPQGTFTEAALMQVPGAADATRIPCTNVNTALERVRAGEADAAM
VPIENSVEGGVTATLDAIATGQELRIIREALVPITFVLVARPGVELSDIK
RISTHGHAWAQCRLWVDEHLPNADYVPGSSTAASAMGLLEDDAPYEAAIC
APLIAAEQPGLNVLAEDIGDNPDAVTRFILVSRPGALPERTGADKTTVVV
PLPEDHPGALMEILDQFASRGVNLSRIESRPTGQYLGHYFFSIDADGHAT
DSRVADALAGLHRISPATRFLGSYARADKQPAVVAPHTSDAAFASAHAWV
DSILKG
3D structure
PDB3mwb The Crystal Structure of Prephenate dehydratase in complex with L-Phe from Arthrobacter aurescens to 2.0A
ChainA
Resolution2.0 Å
3D
structure
Catalytic site residues are labeled in the structure
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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.
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 PHE A N226 L227 S228 R229 N223 L224 S225 R226
BS02 PHE A D208 H209 L213 S232 F244 D205 H206 L210 S229 F241
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

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Molecular Function
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Cellular Component
External links
PDB RCSB:3mwb, PDBe:3mwb, PDBj:3mwb
PDBsum3mwb
PubMed
UniProtA1R118

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