Structure of PDB 7ney Chain A

Receptor sequence
>7neyA (length=497) Species: 452589 (Trichoderma atroviride IMI 206040) [Search protein sequence]
EPPHLSFRSFVEALRQDNDLVDINEPVDPDLEAAAITRLVCETDDKAPLF
NNVIGAKDGLWRILGAPASLRSSPKERFGRLARHLALPPTASAKDILDKM
LSANSIPPIEPVIVPTGPVKENSIEGENIDLEALPAPMVHQSDGGKYIQT
YGMHVIQSPDGCWTNWSIARAMVSGKRTLAGLVISPQHIRKIQDQWRAIG
QEEIPWALAFGVPPTAIMASSMPIPDGVSEAGYVGAIAGEPIKLVKCDTN
NLYVPANSEIVLEGTLSTTKMAPEGPFGEMHGYVYPGESHPGPVYTVNKI
TYRNNAILPMSACGRLTDETQTMIGTLAAAEIRQLCQDAGLPITDAFAPF
VGQATWVALKVDTKRLRAMKTNGKAFAKRVGDVVFTQKPGFTIHRLILVG
DDIDVYDDKDVMWAFTTRCRPGTDEVFFDDVVGFQLIPYMSHGNAEAIKG
GKVVSDALLTAEYTTGKDWESADFKNSYPKSIQDKVLNSWERLGFKK
3D structure
PDB7ney Directed evolution of prenylated FMN-dependent Fdc supports efficient in vivo isobutene production.
ChainA
Resolution1.74 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 T163 N178 I181 A182 R183 Q200 H201 S233 S234 M235 P236 I337 K401 T150 N165 I168 A169 R170 Q187 H188 S220 S221 M222 P223 I324 K388
BS02 MN A N178 H201 E243 N165 H188 E230
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
Cellular Component
GO:0005737 cytoplasm

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Molecular Function
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Cellular Component
External links
PDB RCSB:7ney, PDBe:7ney, PDBj:7ney
PDBsum7ney
PubMed34489427
UniProtG9NLP8

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