Structure of PDB 2vsu Chain A

Receptor sequence
>2vsuA (length=240) Species: 294 (Pseudomonas fluorescens) [Search protein sequence]
YEGRWKTVKVEIEDGIAFVILNRPEKRNAMSPTLNREMIDVLETLEQDPA
AGVLVLTGAGEAWTAGMDLKEAGPEILQEKIRREASQWQWKLLRMYAKPT
IAMVNGWCFGGGFAPLVACDLAICADEATFGLSEINWGIPPGNLVSKAMA
DTVGHRQSLYYIMTGKTFGGQKAAEMGLVNESVPLAQLREVTIELARNLL
EKNPVVLRAAKHGFKRCRELTWEQNEDYLYAKLDQSRLLD
3D structure
PDB2vsu A Ternary Complex of Hydroxycinnamoyl-Coa Hydratase-Lyase (Hchl) with Acetyl-Coa and Vanillin Gives Insights Into Substrate Specificity and Mechanism.
ChainA
Resolution1.9 Å
3D
structure
Catalytic site residues are labeled in the structure
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Enzymatic activity
Catalytic site (original residue number in PDB) M70 R92 Q96 G120 A123 S142 E143 I148 P150 G151 Y239 D249
Catalytic site (residue number reindexed from 1) M67 R83 Q87 G111 A114 S133 E134 I139 P141 G142 Y230 D240
Enzyme Commision number 4.1.2.61: feruloyl-CoA hydratase/lyase.
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 ACO A E28 K29 A32 A68 G69 M70 D71 L72 W116 F118 G119 G120 S142 E143 E25 K26 A29 A65 G66 M67 D68 L69 W107 F109 G110 G111 S133 E134
Gene Ontology
Molecular Function
GO:0003824 catalytic activity
GO:0016829 lyase activity
GO:0050547 feruloyl-CoA hydratase/lyase activity
Biological Process
GO:0008300 isoprenoid catabolic process

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Molecular Function
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Biological Process
External links
PDB RCSB:2vsu, PDBe:2vsu, PDBj:2vsu
PDBsum2vsu
PubMed18479250
UniProtO69762|HCHL_PSEFL Hydroxycinnamoyl-CoA hydratase-lyase

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