Structure of PDB 7nf4 Chain B

Receptor sequence
>7nf4B (length=495) Species: 425011 (Aspergillus niger CBS 513.88) [Search protein sequence]
PAHLCFRSFVEALKVDNDLVEINTPIDPNLEAAAITRRVCETNDKAPLFN
NLIGMKNGLFRILGAPGSLRKSSADRYGRLARHLALPPTASMREILDKML
SASDMPPIPPTIVPTGPCKENSLDDSEFDLTELPVPLIHKSDGGKYIQTY
GMHIVQSPDGTWTNWSIARAMVHDKNHLTGLVIPPQHIWQIHQMWKKEGR
SDVPWALAFGVPPAAIMASSMPIPDGVTEAGYVGAMTGSSLELVKCDTND
LYVPATSEIVLEGTLSISETGPEGPFGEMHGYIFPGDTHLGAKYKVNRIT
YRNNAIMPMSSCGRLTDETHTMIGSLAAAEIRKLCQQNDLPITDAFAPFE
SQVTWVALRVDTEKLRAMKTTSEGFRKRVGDVVFNHKAGYMIHRLVLVGD
DIDVYEGKDVLWAFSTRCRPGMDETLFEDVPGFWLIPYMGHGNGPAHRGG
KVVSDALMPTEYTTGRNWEAADFNQSYPEDLKQKVLDNWTKMGFS
3D structure
PDB7nf4 Directed evolution of prenylated FMN-dependent Fdc supports efficient in vivo isobutene production.
ChainB
Resolution1.69 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 MN B N168 H191 E233 N164 H187 E229
BS02 BYN B T153 N168 I171 A172 R173 Q190 H191 S223 S224 M225 P226 E282 I327 K391 T149 N164 I167 A168 R169 Q186 H187 S219 S220 M221 P222 E278 I323 K387
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:7nf4, PDBe:7nf4, PDBj:7nf4
PDBsum7nf4
PubMed34489427
UniProtA2QHE5|FDC1_ASPNC Ferulic acid decarboxylase 1 (Gene Name=fdc1)

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