Structure of PDB 2r5e Chain B Binding Site BS01

Receptor Information
>2r5e Chain B (length=419) Species: 7159 (Aedes aegypti) [Search protein sequence] [Download receptor structure] [Download structure with residue number starting from 1] [View receptor structure]
NKFDLPKRYQGSTKSVWVEYIQLAAQYKPLNLGQGFPDYHAPKYALNALA
AAANSPDPLANQYTRGFGHPRLVQALSKLYSQLVDRTINPMTEVLVTVGA
YEALYATIQGHVDEGDEVIIIEPFFDCYEPMVKAAGGIPRFIPLKPNKTG
GTISSADWVLDNNELEALFNEKTKMIIINTPHNPLGKVMDRAELEVVANL
CKKWNVLCVSDEVYEHMVFEPFEHIRICTLPGMWERTITIGSAGKTFSLT
GWKIGWAYGPEALLKNLQMVHQNCVYTCATPIQEAIAVGFETELKRLKSP
ECYFNSISGELMAKRDYMASFLAEVGMNPTVPQGGYFMVADWSSLDSKVD
LTQETDARKDYRFTKWMTKSVGLQGIPPSAFYSEPNKHLGEDFVRYCFFK
KDENLQKAAEILRKWKGSS
Ligand information
Ligand IDQLP
InChIInChI=1S/C13H20N3O8P/c1-7-12(18)9(8(4-15-7)6-24-25(21,22)23)5-16-10(13(19)20)2-3-11(14)17/h4,10,16,18H,2-3,5-6H2,1H3,(H2,14,17)(H,19,20)(H2,21,22,23)/t10-/m0/s1
InChIKeyTUUVENFNODJVKV-JTQLQIEISA-N
SMILES
SoftwareSMILES
CACTVS 3.341Cc1ncc(CO[P](O)(O)=O)c(CN[C@@H](CCC(N)=O)C(O)=O)c1O
OpenEye OEToolkits 1.5.0Cc1c(c(c(cn1)COP(=O)(O)O)CN[C@@H](CCC(=O)N)C(=O)O)O
OpenEye OEToolkits 1.5.0Cc1c(c(c(cn1)COP(=O)(O)O)CNC(CCC(=O)N)C(=O)O)O
CACTVS 3.341Cc1ncc(CO[P](O)(O)=O)c(CN[CH](CCC(N)=O)C(O)=O)c1O
ACDLabs 10.04O=C(O)C(NCc1c(cnc(c1O)C)COP(=O)(O)O)CCC(=O)N
FormulaC13 H20 N3 O8 P
NameN~2~-({3-HYDROXY-2-METHYL-5-[(PHOSPHONOOXY)METHYL]PYRIDIN-4-YL}METHYL)-L-GLUTAMINE;
N-({3-HYDROXY-2-METHYL-5-[(PHOSPHONOOXY)METHYL]PYRIDIN-4-YL}METHYL)-L-GLUTAMINE
ChEMBL
DrugBank
ZINCZINC000016052507
PDB chain2r5e Chain A Residue 430 [Download ligand structure] [Download structure with residue number starting from 1] [View ligand structure]
Receptor-Ligand Complex Structure
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PDB2r5e Structural insight into the mechanism of substrate specificity of aedes kynurenine aminotransferase.
Resolution1.84 Å
Binding residue
(original residue number in PDB)		Y73 Y286
Binding residue
(residue number reindexed from 1)		Y63 Y276
Annotation score1
Enzymatic activity
Catalytic site (original residue number in PDB) F135 D221 V223 K255
Catalytic site (residue number reindexed from 1) F125 D211 V213 K245
Enzyme Commision number 2.6.1.-
2.6.1.63: kynurenine--glyoxylate transaminase.
2.6.1.7: kynurenine--oxoglutarate transaminase.
Gene Ontology
Molecular Function
GO:0008483 transaminase activity
GO:0016212 kynurenine-oxoglutarate transaminase activity
GO:0030170 pyridoxal phosphate binding
GO:0047315 kynurenine-glyoxylate transaminase activity
Biological Process
GO:0009058 biosynthetic process
GO:0097053 L-kynurenine catabolic process
Cellular Component
GO:0005737 cytoplasm
GO:0005739 mitochondrion

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Molecular Function
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Biological Process
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Cellular Component
External links
PDB RCSB:2r5e, PDBe:2r5e, PDBj:2r5e
PDBsum2r5e
PubMed18186649
UniProtQ17CS8|KAT_AEDAE Kynurenine aminotransferase (Gene Name=KAT)

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