Structure of PDB 3uha Chain A

Receptor sequence
>3uhaA (length=365) Species: 559292 (Saccharomyces cerevisiae S288C) [Search protein sequence]
AVTLHLRAETKPLEARAALTPTTVKKLIAKGFKIYVEDSPQSTFNINEYR
QAGAIIVPAGSWKTAPRDRIIIGLKEMPETDTFPLVHEHIQFAHCYKDQA
GWQNVLMRFIKGHGTLYDLEFLENDQGRRVAAFGFYAGFAGAALGVRDWA
FKQTHSDDEDLPAVSPYPNEKALVKDVTKDYKEALATGARKPTVLIIGAL
GRSGSGAIDLLHKVGIPDANILKWDIKETSRGGPFDEIPQADIFINCIYL
SKPIAPFTNMEKLNNPNRRLRTVVDVSADTTNPHNPIPIYTVATVFNKPT
VLVPTTAGPKLSVISIDHLPSLLPREASEFFSHDLLPSLELLPQRKTAPV
WVRAKKLFDRHCARV
3D structure
PDB3uha Evidence in Support of Lysine 77 and Histidine 96 as Acid-Base Catalytic Residues in Saccharopine Dehydrogenase from Saccharomyces cerevisiae.
ChainA
Resolution2.3 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 NAD A R130 A139 G200 G203 R204 S205 D227 I228 T231 I250 Y251 V278 D319 H320 L321 R128 A137 G198 G201 R202 S203 D225 I226 T229 I248 Y249 V276 D317 H318 L319
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:3uha, PDBe:3uha, PDBj:3uha
PDBsum3uha
PubMed22243403
UniProtP38998|LYS1_YEAST Saccharopine dehydrogenase [NAD(+), L-lysine-forming] (Gene Name=LYS1)

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