Structure of PDB 5vep Chain A

Receptor sequence

>5vepA (length=410) Species: 10090 (Mus musculus)

NAKRIEGLDSNVWVEFTKLAADPSVVNLGQGFPDISPPSYVKEELSKAAF
IDNMNQYTRGFGHPALVKALSCLYGKIYQRQIDPNEEILVAVGAYGSLFN
SIQGLVDPGDEVIIMVPFYDCYEPMVRMAGAVPVFIPLRSKPTDGMKWTS
SDWTFDPRELESKFSSKTKAIILNTPHNPLGKVYTRQELQVIADLCVKHD
TLCISDEVYEWLVYTGHTHVKIATLPGMWERTITIGSAGKTFSVTGWKLG
WSIGPAHLIKHLQTVQQNSFYTCATPLQAALAEAFWIDIKRMDDPECYFN
SLPKELEVKRDRMVRLLNSVGLKPIVPDGGYFIIADVSSLGADLSDMNSD
EPYDYKFVKWMTKHKKLTAIPVSAFCDSKSKPHFEKLVRFCFIKKDSTLD
AAEEIFRAWN

3D structure

• PDB: 5vep Detect, correct, retract: How to manage incorrect structural models.
• Chain: A
• Resolution: 2.59 Å

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	CA	A	H240 D241	H199 D200
BS02	CA	A	N42 E47	N1 E6

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

External links

• PDB: RCSB:5vep, PDBe:5vep, PDBj:5vep
• PDBsum: 5vep
• PubMed: 29113027
• UniProt: Q71RI9|KAT3_MOUSE Kynurenine--oxoglutarate transaminase 3 (Gene Name=Kyat3)