Structure of PDB 2r5e Chain B

Receptor sequence
>2r5eB (length=419) Species: 7159 (Aedes aegypti) [Search protein sequence]
NKFDLPKRYQGSTKSVWVEYIQLAAQYKPLNLGQGFPDYHAPKYALNALA
AAANSPDPLANQYTRGFGHPRLVQALSKLYSQLVDRTINPMTEVLVTVGA
YEALYATIQGHVDEGDEVIIIEPFFDCYEPMVKAAGGIPRFIPLKPNKTG
GTISSADWVLDNNELEALFNEKTKMIIINTPHNPLGKVMDRAELEVVANL
CKKWNVLCVSDEVYEHMVFEPFEHIRICTLPGMWERTITIGSAGKTFSLT
GWKIGWAYGPEALLKNLQMVHQNCVYTCATPIQEAIAVGFETELKRLKSP
ECYFNSISGELMAKRDYMASFLAEVGMNPTVPQGGYFMVADWSSLDSKVD
LTQETDARKDYRFTKWMTKSVGLQGIPPSAFYSEPNKHLGEDFVRYCFFK
KDENLQKAAEILRKWKGSS
3D structure
PDB2r5e Structural insight into the mechanism of substrate specificity of aedes kynurenine aminotransferase.
ChainB
Resolution1.84 Å
3D
structure
Catalytic site residues are labeled in the structure
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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.
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 QLP B Y73 Y286 Y63 Y276
BS02 QLP B W27 Q44 G109 A110 Y111 F135 N189 N193 D221 Y224 S252 K255 K263 F347 R405 W17 Q34 G99 A100 Y101 F125 N179 N183 D211 Y214 S242 K245 K253 F337 R395
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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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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