Structure of PDB 2vsu Chain F

Receptor sequence
>2vsuF (length=245) Species: 294 (Pseudomonas fluorescens) [Search protein sequence]
YEGRWKTVKVEIEDGIAFVILNRPERRNAMSPTLNREMIDVLETLEQDPA
AGVLVLTGAGEAWTAGMDLKEYFREVDAGPEILQEKIRREASQWQWKLLR
MYAKPTIAMVNGWCFGGGFAPLVACDLAICADEATFGLSEINWGIPPGNL
VSKAMADTVGHRQSLYYIMTGKTFGGQKAAEMGLVNESVPLAQLREVTIE
LARNLLEKNPVVLRAAKHGFKRCRELTWEQNEDYLYAKLDQSRLL
3D structure
PDB2vsu A Ternary Complex of Hydroxycinnamoyl-Coa Hydratase-Lyase (Hchl) with Acetyl-Coa and Vanillin Gives Insights Into Substrate Specificity and Mechanism.
ChainF
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 Y75 D80 R92 Q96 G120 A123 S142 E143 I148 P150 G151 Y239
Catalytic site (residue number reindexed from 1) M67 Y72 D77 R89 Q93 G117 A120 S139 E140 I145 P147 G148 Y236
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 F E28 R29 R30 A32 A68 G69 M70 D71 L72 F76 W116 F118 S142 E143 E25 R26 R27 A29 A65 G66 M67 D68 L69 F73 W113 F115 S139 E140
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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