Structure of PDB 2r5c Chain B

Receptor sequence

>2r5cB (length=419) Species: 7159 (Aedes aegypti)

NKFDLPKRYQGSTKSVWVEYIQLAAQYKPLNLGQGFPDYHAPKYALNALA
AAANSPDPLANQYTRGFGHPRLVQALSKLYSQLVDRTINPMTEVLVTVGA
YEALYATIQGHVDEGDEVIIIEPFFDCYEPMVKAAGGIPRFIPLKPNKTG
GTISSADWVLDNNELEALFNEKTKMIIINTPHNPLGKVMDRAELEVVANL
CKKWNVLCVSDEVYEHMVFEPFEHIRICTLPGMWERTITIGSAGKTFSLT
GWKIGWAYGPEALLKNLQMVHQNCVYTCATPIQEAIAVGFETELKRLKSP
ECYFNSISGELMAKRDYMASFLAEVGMNPTVPQGGYFMVADWSSLDSKVD
LTQETDARKDYRFTKWMTKSVGLQGIPPSAFYSEPNKHLGEDFVRYCFFK
KDENLQKAAEILRKWKGSS

3D structure

• PDB: 2r5c Structural insight into the mechanism of substrate specificity of aedes kynurenine aminotransferase.
• Chain: B
• Resolution: 1.96 Å

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	C6P	B	W27 G45 G109 A110 Y111 F135 N189 N193 D221 Y224 S252 K255 K263 F347 R405	W17 G35 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

External links

• PDB: RCSB:2r5c, PDBe:2r5c, PDBj:2r5c
• PDBsum: 2r5c
• PubMed: 18186649
• UniProt: Q17CS8|KAT_AEDAE Kynurenine aminotransferase (Gene Name=KAT)