Structure of PDB 3mwb Chain B

Receptor sequence
>3mwbB (length=303) Species: 290340 (Paenarthrobacter aurescens TC1) [Search protein sequence]
VTYTFLGPQGTFTEAALMQVPGAADATRIPCTNVNTALERVRAGEADAAM
VPIENSVEGGVTATLDAIATGQELRIIREALVPITFVLVARPGVELSDIK
RISTHGHAWAQCRLWVDEHLPNADYVPGSSTAASAMGLLEDDAPYEAAIC
APLIAAEQPGLNVLAEDIGDNPDAVTRFILVSRPGALPERTGADKTTVVV
PLPEDHPGALMEILDQFASRGVNLSRIESRPTLGHYFFSIDADGHATDSR
VADALAGLHRISPATRFLGSYARADKQPAVVAPHTSDAAFASAHAWVDSI
LKG
3D structure
PDB3mwb The Crystal Structure of Prephenate dehydratase in complex with L-Phe from Arthrobacter aurescens to 2.0A
ChainB
Resolution2.0 Å
3D
structure
Catalytic site residues are labeled in the structure
[Spin on]
[Spin off]
[Reset orientation]

[High quality]
[Low quality]

[White background]
[Black background]

[Download]
[Download structure with residue number starting from 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.
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 B D208 H209 L213 Y242 F244 D205 H206 L210 Y236 F238
BS02 PHE B N226 L227 S228 R229 I230 N223 L224 S225 R226 I227
BS03 MG B A158 Q161 L164 A155 Q158 L161
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

View graph for
Molecular Function
View graph for
Biological Process
View graph for
Cellular Component
External links
PDB RCSB:3mwb, PDBe:3mwb, PDBj:3mwb
PDBsum3mwb
PubMed
UniProtA1R118

[Back to BioLiP]