Structure of PDB 3e2y Chain B

Receptor sequence
>3e2yB (length=410) Species: 10090 (Mus musculus) [Search protein sequence]
NAKRIEGLDSNVWVEFTKLAADPSVVNLGQGFPDISPPSYVKEELSKAAF
IDNMNQYTRGFGHPALVKALSCLYGKIYQRQIDPNEEILVAVGAYGSLFN
SIQGLVDPGDEVIIMVPFYDCYEPMVRMAGAVPVFIPLRSKPTDGMKWTS
SDWTFDPRELESKFSSKTKAIILNTPHNPLGKVYTRQELQVIADLCVKHD
TLCISDEVYEWLVYTGHTHVKIATLPGMWERTITIGSAGKTFSVTGWKLG
WSIGPAHLIKHLQTVQQNSFYTCATPLQAALAEAFWIDIKRMDDPECYFN
SLPKELEVKRDRMVRLLNSVGLKPIVPDGGYFIIADVSSLGADLSDMNSD
EPYDYKFVKWMTKHKKLTAIPVSAFCDSKSKPHFEKLVRFCFIKKDSTLD
AAEEIFRAWN
3D structure
PDB3e2y Correction for Han et al., "Biochemical and Structural Properties of Mouse Kynurenine Aminotransferase III".
ChainB
Resolution2.26 Å
3D
structure
Catalytic site residues are labeled in the structure
[Spin on]
[Spin off]
[Reset orientation]

[High quality]
[Low quality]

[White background]
[Black background]

[Download]
[Download structure with residue number starting from 1]
Enzymatic activity
Catalytic site (original residue number in PDB) Y160 D247 V249 K281
Catalytic site (residue number reindexed from 1) Y119 D206 V208 K240
Enzyme Commision number 2.6.1.63: kynurenine--glyoxylate transaminase.
2.6.1.7: kynurenine--oxoglutarate transaminase.
4.4.1.13: cysteine-S-conjugate beta-lyase.
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 PMP B G134 A135 Y136 Y160 N215 D247 Y250 S278 K281 K289 G93 A94 Y95 Y119 N174 D206 Y209 S237 K240 K248
BS02 GLN B W54 G72 R430 W13 G31 R389
Gene Ontology
Molecular Function
GO:0008483 transaminase activity
GO:0016212 kynurenine-oxoglutarate transaminase activity
GO:0016829 lyase activity
GO:0030170 pyridoxal phosphate binding
GO:0042803 protein homodimerization activity
GO:0047315 kynurenine-glyoxylate transaminase activity
GO:0047804 cysteine-S-conjugate beta-lyase activity
Biological Process
GO:0006103 2-oxoglutarate metabolic process
GO:0006520 amino acid metabolic process
GO:0009058 biosynthetic process
GO:0070189 kynurenine metabolic process
GO:0097053 L-kynurenine catabolic process
Cellular Component
GO:0005739 mitochondrion

View graph for
Molecular Function

View graph for
Biological Process

View graph for
Cellular Component
External links
PDB RCSB:3e2y, PDBe:3e2y, PDBj:3e2y
PDBsum3e2y
PubMed29712768
UniProtQ71RI9|KAT3_MOUSE Kynurenine--oxoglutarate transaminase 3 (Gene Name=Kyat3)

[Back to BioLiP]