Structure of PDB 7nf3 Chain A

Receptor sequence
>7nf3A (length=498) Species: 425011 (Aspergillus niger CBS 513.88) [Search protein sequence]
QPAHLCFRSFVEALKVDNDLVEINTPIDPNLEAAAITRRVCETNDKAPLF
NNLIGMKNGLFRILGAPGSLRKSSADRYGRLARHLALPPTASMREILDKM
LSASDMPPIPPTIVPTGPCKENSLDDSEFDLTELPVPLIHKSDGGKYIQT
YGMHIVQSPDGTWTNWSIARAMVHDKNHLTGLVIPPQHIWQIHQMWKKEG
RSDVPWALAFGVPPAAIMASSMPIPDGVTEAGYVGAMTGSSLELVKCDTN
DLYVPATSEIVLEGTLSISETGPEGPFGEMHGYIFPGDTHLGAKYKVNRI
TYRNNAIMPMSSCGRLTDETHTMIGSLAAAEIRKLCQQNDLPITDAFAPF
ESQVTWVALRVDTEKLRAMKTTSEGFRKRVGDVVFNHKAGYMIHRLVLVG
DDIDVYEGKDVLWAFSTRCRPGMDETLFEDVRGFPLIPYMGHGNGPAHRG
GKVVSDALMPTEYTTGRNWEAADFNQSYPEDLKQKVLDNWTKMGFSHH
3D structure
PDB7nf3 Directed evolution of prenylated FMN-dependent Fdc supports efficient in vivo isobutene production.
ChainA
Resolution1.1 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 A T153 N168 S170 I171 A172 R173 Q190 H191 S223 S224 M225 P226 I327 K391 T150 N165 S167 I168 A169 R170 Q187 H188 S220 S221 M222 P223 I324 K388
BS02 MN A N168 H191 E233 N165 H188 E230
Gene Ontology
Molecular Function
GO:0016831 carboxy-lyase activity
GO:0030145 manganese ion binding
GO:0042802 identical protein binding
GO:0046872 metal ion binding
Biological Process
GO:0009074 aromatic amino acid family catabolic process
GO:0018966 styrene metabolic process
GO:0033494 ferulate metabolic process
GO:0046281 cinnamic acid catabolic process
Cellular Component
GO:0005737 cytoplasm

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Cellular Component
External links
PDB RCSB:7nf3, PDBe:7nf3, PDBj:7nf3
PDBsum7nf3
PubMed34489427
UniProtA2QHE5|FDC1_ASPNC Ferulic acid decarboxylase 1 (Gene Name=fdc1)

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