Structure of PDB 6evf Chain D

Receptor sequence
>6evfD (length=501) Species: 559292 (Saccharomyces cerevisiae S288C) [Search protein sequence]
KLNPALEFRDFIQVLKDEDDLIEITEEIDPNLEVGAIMRKAYESHLPAPL
FKNLKGASKDLFSILGCPAGLRSKEKGDHGRIAHHLGLDPKTTIKEIIDY
LLECKEKEPLPPITVPVSSAPCKTHILSEEKIHLQSLPTPYLHVSDGGKY
LQTYGMWILQTPDKKWTNWSIARGMVVDDKHITGLVIKPQHIRQIADSWA
AIGKANEIPFALCFGVPPAAILVSSMPIPEGVSESDYVGAILGESVPVVK
CETNDLMVPATSEMVFEGTLSLTDTHLEGPFGDMHGYVFKSQGHPCPLYT
VKAMSYRDNAILPVSNPGLCTDETHTLIGSLVATEAKELAIESGLPILDA
FMPYEAQALWLILKVDLKGLQALKTTPEEFCKKVGDIYFRTKVGFIVHEI
ILVADDIDIFNFKEVIWAYVTRHTPVADQMAFDDVTSFPLAPFVSQSSRS
KTMKGGKCVTNCIFRQQYERSFDYITCNFEKGYPKGLVDKVNENWKRYGY
K
3D structure
PDB6evf The role of conserved residues in Fdc decarboxylase in prenylated flavin mononucleotide oxidative maturation, cofactor isomerization, and catalysis.
ChainD
Resolution2.06 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 R175 Q192 H193 S226 S227 M228 P229 S317 I330 T153 N168 S170 I171 A172 R173 Q190 H191 S224 S225 M226 P227 S315 I328
BS02 MN D N170 H193 E236 N168 H191 E234
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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Cellular Component
External links
PDB RCSB:6evf, PDBe:6evf, PDBj:6evf
PDBsum6evf
PubMed29259125
UniProtQ03034|FDC1_YEAST Ferulic acid decarboxylase 1 (Gene Name=FDC1)

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