Structure of PDB 2qrj Chain A

Receptor sequence
>2qrjA (length=365) Species: 4932 (Saccharomyces cerevisiae) [Search protein sequence]
AVTLHLRAETKPLEARAALTPTTVKKLIAKGFKIYVEDSPQSTFNINEYR
QAGAIIVPAGSWKTAPRDRIIIGLKEMPETDTFPLVHEHIQFAHCYKDQA
GWQNVLMRFIKGHGTLYDLEFLENDQGRRVAAFGFYAGFAGAALGVRDWA
FKQTHSDDEDLPAVSPYPNEKALVKDVTKDYKEALATGARKPTVLIIGAL
GRCGSGAIDLLHKVGIPDANILKWDIKETSRGGPFDEIPQADIFINCIYL
SKPIAPFTNMEKLNNPNRRLRTVVDVSADTTNPHNPIPIYTVATVFNKPT
VLVPTTAGPKLSVISIDHLPSLLPREASEFFSHDLLPSLELLPQRKTAPV
WVRAKKLFDRHCARV
3D structure
PDB2qrj Crystal Structures of Ligand-Bound Saccharopine Dehydrogenase from Saccharomyces cerevisiae
ChainA
Resolution1.6 Å
3D
structure
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Enzymatic activity
Enzyme Commision number 1.5.1.7: saccharopine dehydrogenase (NAD(+), L-lysine-forming).
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 SO4 A R131 A134 F135 R129 A132 F133
BS02 SO4 A K35 Y37 R71 K33 Y35 R69
Gene Ontology
Molecular Function
GO:0003729 mRNA binding
GO:0004753 saccharopine dehydrogenase activity
GO:0004754 saccharopine dehydrogenase (NAD+, L-lysine-forming) activity
GO:0005515 protein binding
GO:0016491 oxidoreductase activity
Biological Process
GO:0006553 lysine metabolic process
GO:0009085 lysine biosynthetic process
GO:0016558 protein import into peroxisome matrix
GO:0019878 lysine biosynthetic process via aminoadipic acid
Cellular Component
GO:0005737 cytoplasm
GO:0005777 peroxisome

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Molecular Function
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Biological Process
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Cellular Component
External links
PDB RCSB:2qrj, PDBe:2qrj, PDBj:2qrj
PDBsum2qrj
PubMed17939687
UniProtP38998|LYS1_YEAST Saccharopine dehydrogenase [NAD(+), L-lysine-forming] (Gene Name=LYS1)

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