Structure of PDB 2vss Chain D

Receptor sequence
>2vssD (length=246) Species: 294 (Pseudomonas fluorescens) [Search protein sequence]
TYEGRWKTVKVEIEDGIAFVILNRPEKRNAMSPTLNREMIDVLETLEQDP
AAGVLVLTGAGEAWTAGMDLKEYFREVDAGPEILQEKIRREASQWQWKLL
RMYAKPTIAMVNGWCFGGGFSPLVACDLAICADEATFGLSEINWGIPPGN
LVSKAMADTVGHRQSLYYIMTGKTFGGQKAAEMGLVNESVPLAQLREVTI
ELARNLLEKNPVVLRAAKHGFKRCRELTWEQNEDYLYAKLDQSRLL
3D structure
PDB2vss A Ternary Complex of Hydroxycinnamoyl-Coa Hydratase-Lyase (Hchl) with Acetyl-Coa and Vanillin Gives Insights Into Substrate Specificity and Mechanism.
ChainD
Resolution2.22 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 S123 S142 E143 I148 P150 G151 Y239
Catalytic site (residue number reindexed from 1) M68 Y73 D78 R90 Q94 G118 S121 S140 E141 I146 P148 G149 Y237
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 D E28 K29 R30 A32 A68 M70 D71 L72 F76 W116 F118 S142 E26 K27 R28 A30 A66 M68 D69 L70 F74 W114 F116 S140
BS02 V55 D M70 Y75 F76 Q98 E143 G151 N152 M68 Y73 F74 Q96 E141 G149 N150
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:2vss, PDBe:2vss, PDBj:2vss
PDBsum2vss
PubMed18479250
UniProtO69762|HCHL_PSEFL Hydroxycinnamoyl-CoA hydratase-lyase

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