Structure of PDB 1e5q Chain A Binding Site BS02

Receptor Information
>1e5q Chain A (length=449) Species: 148305 (Pyricularia grisea) [Search protein sequence] [Download receptor structure] [Download structure with residue number starting from 1] [View receptor structure]
ATKSVLMLGSGFVTRPTLDVLTDSGIKVTVACRTLESAKKLSAGVQHSTP
ISLDVNDDAALDAEVAKHDLVISLIPYTFHATVIKSAIRQKKHVVTTSYV
SPAMMELDQAAKDAGITVMNEIGLDPGIDHLYAIKTIEEVHAAGGKIKTF
LSYCGGLPAPESSDNPLGYKFSWSSRGVLLALRNAASFYKDGKVTNVAGP
ELMATAKPYFIYPGFAFVAYPNRDSTPYKERYQIPEADNIVRGTLRYQGF
PQFIKVLVDIGFLSDEEQPFLKEAIPWKEATQKIVKASSASEQDIVSTIV
SNATFESTEEQKRIVAGLKWLGIFSDKKITPRGNALDTLCATLEEKMQFE
EGERDLVMLQHKFEIENKDGSRETRTSSLCEYGAPIGSGGYSAMAKLVGV
PCAVAVKFVLDGTISDRGVLAPMNSKINDPLMKELKEKYGIECKEKVVA
Ligand information
Ligand IDSHR
InChIInChI=1S/C11H20N2O6/c12-7(10(16)17)3-1-2-6-13-8(11(18)19)4-5-9(14)15/h7-8,13H,1-6,12H2,(H,14,15)(H,16,17)(H,18,19)/t7-,8-/m0/s1
InChIKeyZDGJAHTZVHVLOT-YUMQZZPRSA-N
SMILES
SoftwareSMILES
CACTVS 3.341N[C@@H](CCCCN[C@@H](CCC(O)=O)C(O)=O)C(O)=O
OpenEye OEToolkits 1.5.0C(CCN[C@@H](CCC(=O)O)C(=O)O)C[C@@H](C(=O)O)N
ACDLabs 10.04O=C(O)C(N)CCCCNC(C(=O)O)CCC(=O)O
OpenEye OEToolkits 1.5.0C(CCNC(CCC(=O)O)C(=O)O)CC(C(=O)O)N
CACTVS 3.341N[CH](CCCCN[CH](CCC(O)=O)C(O)=O)C(O)=O
FormulaC11 H20 N2 O6
NameN-(5-AMINO-5-CARBOXYPENTYL)GLUTAMIC ACID
ChEMBL
DrugBankDB04207
ZINCZINC000001532666
PDB chain1e5q Chain A Residue 501 [Download ligand structure] [Download structure with residue number starting from 1] [View ligand structure]
Receptor-Ligand Complex Structure
Global viewLocal viewStructure summary

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PDB1e5q Crystal Structure of Saccharopine Reductase from Magnaporthe Grisea, an Enzyme of the Alpha-Aminoadipate Pathway of Lysine Biosynthesis
Resolution2.1 Å
Binding residue
(original residue number in PDB)		Y78 S99 Y100 D126 C155 G156 W174 R224 T245 R247
Binding residue
(residue number reindexed from 1)		Y77 S98 Y99 D125 C154 G155 W173 R223 T244 R246
Annotation score5
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).
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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