Structure of PDB 1e5q Chain F

Receptor sequence
>1e5qF (length=449) Species: 148305 (Pyricularia grisea) [Search protein sequence]
ATKSVLMLGSGFVTRPTLDVLTDSGIKVTVACRTLESAKKLSAGVQHSTP
ISLDVNDDAALDAEVAKHDLVISLIPYTFHATVIKSAIRQKKHVVTTSYV
SPAMMELDQAAKDAGITVMNEIGLDPGIDHLYAIKTIEEVHAAGGKIKTF
LSYCGGLPAPESSDNPLGYKFSWSSRGVLLALRNAASFYKDGKVTNVAGP
ELMATAKPYFIYPGFAFVAYPNRDSTPYKERYQIPEADNIVRGTLRYQGF
PQFIKVLVDIGFLSDEEQPFLKEAIPWKEATQKIVKASSASEQDIVSTIV
SNATFESTEEQKRIVAGLKWLGIFSDKKITPRGNALDTLCATLEEKMQFE
EGERDLVMLQHKFEIENKDGSRETRTSSLCEYGAPIGSGGYSAMAKLVGV
PCAVAVKFVLDGTISDRGVLAPMNSKINDPLMKELKEKYGIECKEKVVA
3D structure
PDB1e5q Crystal Structure of Saccharopine Reductase from Magnaporthe Grisea, an Enzyme of the Alpha-Aminoadipate Pathway of Lysine Biosynthesis
ChainF
Resolution2.1 Å
3D
structure
Catalytic site residues are labeled in the structure
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Enzymatic activity
Catalytic site (original residue number in PDB) D126
Catalytic site (residue number reindexed from 1) D125
Enzyme Commision number 1.5.1.10: saccharopine dehydrogenase (NADP(+), L-glutamate-forming).
Interaction with ligand
Gene Ontology
Molecular Function
GO:0004753 saccharopine dehydrogenase activity
GO:0004755 saccharopine dehydrogenase (NADP+, L-glutamate-forming) activity
GO:0016491 oxidoreductase activity
Biological Process
GO:0006553 lysine metabolic process
GO:0009085 lysine biosynthetic process
GO:0019878 lysine biosynthetic process via aminoadipic acid
Cellular Component
GO:0005575 cellular_component
GO:0005737 cytoplasm

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Molecular Function
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Biological Process
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Cellular Component
External links
PDB RCSB:1e5q, PDBe:1e5q, PDBj:1e5q
PDBsum1e5q
PubMed11080625
UniProtQ9P4R4|LYS9_PYRO7 Saccharopine dehydrogenase [NADP(+), L-glutamate-forming] (Gene Name=LYS3)

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