Structure of PDB 5z0c Chain A

Receptor sequence
>5z0cA (length=367) Species: 488003 (Persicaria minor) [Search protein sequence]
EEHTVKAVGWAARDPSGHLSPFTFSRRATGELDVTFKVLYCGICHSDLHY
IKNEWSNTIYPALPGHEIVGEVTEVGSKVNKFKVGDKVGVGCIVGSCHSC
PNCNNHLENYCPNRILTFGSRYYDGTLNHGGYSDLMVVQEHFAVRIPDAL
PLDSAAPLLCAGITVYSPLRYYGLDKPGLHVGVVGLGGLGHMAVKFAKAF
GVKVTVVSTSPAKKEDAISGLGAHSFILSTDAEQMQAAVGTMDGIIDTVS
ASHPLPPLISLLKSHGKLVMVGDPPKPLELPVFPLLLGRKMVAGSAIGGM
KETQEMIDFAAKEGVRADVEVIPMDYVNTAMQRVSKSDVKYRFVIDIGNT
FNDSLISSEVEHHHHHH
3D structure
PDB5z0c Structural and kinetic studies of a novel nerol dehydrogenase from Persicaria minor, a nerol-specific enzyme for citral biosynthesis.
ChainA
Resolution1.54 Å
3D
structure
Catalytic site residues are labeled in the structure
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Enzymatic activity
Catalytic site (original residue number in PDB) C51 S53 H56 H73 C167
Catalytic site (residue number reindexed from 1) C44 S46 H49 H66 C160
Enzyme Commision number ?
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 ZN A C104 C107 C110 C118 C97 C100 C103 C111
BS02 ZN A C51 H73 C167 C44 H66 C160
Gene Ontology
Molecular Function
GO:0008270 zinc ion binding
GO:0016491 oxidoreductase activity
GO:0016616 oxidoreductase activity, acting on the CH-OH group of donors, NAD or NADP as acceptor
GO:0045551 cinnamyl-alcohol dehydrogenase activity
GO:0046872 metal ion binding
Biological Process
GO:0009809 lignin biosynthetic process

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Molecular Function
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Biological Process
External links
PDB RCSB:5z0c, PDBe:5z0c, PDBj:5z0c
PDBsum5z0c
PubMed29304481
UniProtJ7JYU1

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