Structure of PDB 6eve Chain B

Receptor sequence
>6eveB (length=499) Species: 559292 (Saccharomyces cerevisiae S288C) [Search protein sequence]
RKLNPALEFRDFIQVLKDEDDLIEITEEIDPNLEVGAIMRKAYESHLPAP
LFKNLKGASKDLFSILGCPAGLRSKEKGDHGRIAHHLGLDPKTTIKEIID
YLLECKEKEPLPPITVPVSSAPCKTHILSEEKIHLQSLPTPYLHVSDGGK
YLQTYGMWILQTPDKKWTNWSIAAGMVVDDKHITGLVIKPQHIRQIADSW
AAIGKANEIPFALCFGVPPAAILVSSMPIPEGVSESDYVGAILGESVPVV
KCETNDLMVPATSEMVFEGTLSLTDTHLEGPFGEMHGYVFKSPCPLYTVK
AMSYRDNAILPVSNPGLCTDETHTLIGSLVATEAKELAIESGLPILDAFM
PYEAQALWLILKVDLKGLQALKTTPEEFCKKVGDIYFRTKVGFIVHEIIL
VADDIDIFNFKEVIWAYVTRHTPVADQMAFDDVTSFPLAPFVSQSSRSKT
MKGGKCVTNCIFRQQYERSFDYITCNFEKGYPKGLVDKVNENWKRYGYK
3D structure
PDB6eve The role of conserved residues in Fdc decarboxylase in prenylated flavin mononucleotide oxidative maturation, cofactor isomerization, and catalysis.
ChainB
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 B T155 N170 I173 A174 Q192 H193 S227 M228 P229 I330 K394 T154 N169 I172 A173 Q191 H192 S226 M227 P228 I326 K390
BS02 MN B N170 H193 E236 N169 H192 E235
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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Molecular Function

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Biological Process

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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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