Structure of PDB 6eve Chain D

Receptor sequence
>6eveD (length=497) Species: 559292 (Saccharomyces cerevisiae S288C) [Search protein sequence]
LNPALEFRDFIQVLKDEDDLIEITEEIDPNLEVGAIMRKAYESHLPAPLF
KNLKGASKDLFSILGCPAGLRSKEKGDHGRIAHHLGLDPKTTIKEIIDYL
LECKEKEPLPPITVPVSSAPCKTHILSEEKIHLQSLPTPYLHVSDGGKYL
QTYGMWILQTPDKKWTNWSIAAGMVVDDKHITGLVIKPQHIRQIADSWAA
IGKANEIPFALCFGVPPAAILVSSMPIPEGVSESDYVGAILGESVPVVKC
ETNDLMVPATSEMVFEGTLSLTDTHLEGPFGEMHGYVFKSPCPLYTVKAM
SYRDNAILPVSNPGLCTDETHTLIGSLVATEAKELAIESGLPILDAFMPY
EAQALWLILKVDLKGLQALKTTPEEFCKKVGDIYFRTKVGFIVHEIILVA
DDIDIFNFKEVIWAYVTRHTPVADQMAFDDVTSFPLAPFVSQSSRSKTMK
GGKCVTNCIFRQQYERSFDYITCNFEKGYPKGLVDKVNENWKRYGYK
3D structure
PDB6eve The role of conserved residues in Fdc decarboxylase in prenylated flavin mononucleotide oxidative maturation, cofactor isomerization, and catalysis.
ChainD
Resolution2.05 Å
3D
structure
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Enzymatic activity
Enzyme Commision number 4.1.1.102: phenacrylate decarboxylase.
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 4LU D T155 N170 S172 I173 A174 A175 Q192 H193 S227 P229 S317 I330 K394 T152 N167 S169 I170 A171 A172 Q189 H190 S224 P226 S311 I324 K388
BS02 MN D N170 H193 E236 N167 H190 E233
BS03 MN D V225 S226 M228 E236 V222 S223 M225 E233
Gene Ontology
Molecular Function
GO:0016831 carboxy-lyase activity
GO:0046872 metal ion binding
Biological Process
GO:0033494 ferulate metabolic process
GO:0046281 cinnamic acid catabolic process
GO:1901067 ferulate catabolic process
Cellular Component
GO:0005737 cytoplasm

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Cellular Component
External links
PDB RCSB:6eve, PDBe:6eve, PDBj:6eve
PDBsum6eve
PubMed29259125
UniProtQ03034|FDC1_YEAST Ferulic acid decarboxylase 1 (Gene Name=FDC1)

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