Structure of PDB 5veq Chain B

Receptor sequence
>5veqB (length=396) Species: 10090 (Mus musculus) [Search protein sequence]
ANAKRIEGLDSNVWVEFDPSVVNLGQGFPDISPPSYVKEELSKAAFIDNM
NQYTRGFGHPALVKALSCLYGKIYQRQIDPNEEILVAVGAYGSLFNSIQG
LVDPGDEVIIMVPFYDCYEPMVRMAGAVPVFIPLRSKPTDGMKWTSSDWT
FDPRELESKFSSKTKAIILNTPHNPLGKVYTRQELQVIADLCVKHDTLCI
SDEVYEWLVYTGHTHVKIATLPGMWERTITIGSAGKTFSVTGWKLGWSIG
PAHLIKHLQTVQQNSFYTCATPLQAALAEAFWIDIKRMDDPECYFNSLPK
ELEVKRDRMVRLLNSVGLKPIVPDGGYFIIADVSSLEPYDYKFVKWMTKH
KKLTAIPVSAFCDSKSKPHFEKLVRFCFIKKDSTLDAAEEIFRAWN
3D structure
PDB5veq Detect, correct, retract: How to manage incorrect structural models.
ChainB
Resolution2.26 Å
3D
structure
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Enzymatic activity
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 N219 D247 Y250 S278 K281 K289 G89 A90 Y91 Y115 N170 N174 D202 Y205 S233 K236 K244
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

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Molecular Function
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Cellular Component
External links
PDB RCSB:5veq, PDBe:5veq, PDBj:5veq
PDBsum5veq
PubMed29113027
UniProtQ71RI9|KAT3_MOUSE Kynurenine--oxoglutarate transaminase 3 (Gene Name=Kyat3)

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