Structure of PDB 2vgz Chain B

Receptor sequence
>2vgzB (length=414) Species: 9606 (Homo sapiens) [Search protein sequence]
MLENYARFITAASAARNPSPSMISLAGGLPNPNMFPFKTAVITVENGKTI
QFGEEMMKRALQYSPSAGIPELLSWLKQLQIKLHNPPTIHYPPSQGQMDL
CVTSGSQQGLCKVFEMIINPGDNVLLDEPAYSGTLQSLHPLGCNIINVAS
DESGIVPDSLRDILSRWKPEDAKNPQKNTPKFLYTVPNGNNPTGNSLTSE
RKKEIYELARKYDFLIIEDDPYYFLQFNKFRVPTFLSMDVDGRVIRADSF
SKIISSGLRIGFLTGPKPLIERVILHIQVSTLHPSTFNQLMISQLLHEWG
EEGFMAHVDRVIDFYSNQKDAILAAADKWLTGLAEWHVPAAGMFLWIKVK
GINDVKELIEEKAVKMGVLMLPGNAFYVDSSAPSPYLRASFSSASPEQMD
VAFQVLAQLIKESL
3D structure
PDB2vgz Crystal Structure of Human Kynurenine Aminotransferase II, a Drug Target for the Treatment of Schizophrenia.
ChainB
Resolution2.3 Å
3D
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Enzymatic activity
Enzyme Commision number 2.6.1.39: 2-aminoadipate transaminase.
2.6.1.4: glycine transaminase.
2.6.1.63: kynurenine--glyoxylate transaminase.
2.6.1.7: kynurenine--oxoglutarate transaminase.
2.6.1.73: methionine--glyoxylate 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 PLP B S117 Q118 Y142 N202 P232 Y233 S260 S262 K263 R270 S106 Q107 Y131 N191 P221 Y222 S249 S251 K252 R259
Gene Ontology
Molecular Function
GO:0008483 transaminase activity
GO:0016212 kynurenine-oxoglutarate transaminase activity
GO:0030170 pyridoxal phosphate binding
GO:0042803 protein homodimerization activity
GO:0047315 kynurenine-glyoxylate transaminase activity
GO:0047536 2-aminoadipate transaminase activity
GO:0047958 glycine:2-oxoglutarate aminotransferase activity
GO:0050094 methionine-glyoxylate transaminase activity
Biological Process
GO:0006103 2-oxoglutarate metabolic process
GO:0006536 glutamate metabolic process
GO:0009058 biosynthetic process
GO:0033512 L-lysine catabolic process to acetyl-CoA via saccharopine
GO:0070189 kynurenine metabolic process
GO:1901605 alpha-amino acid metabolic process
Cellular Component
GO:0005739 mitochondrion
GO:0005759 mitochondrial matrix

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Molecular Function
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Biological Process
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Cellular Component
External links
PDB RCSB:2vgz, PDBe:2vgz, PDBj:2vgz
PDBsum2vgz
PubMed18056996
UniProtQ8N5Z0|AADAT_HUMAN Kynurenine/alpha-aminoadipate aminotransferase, mitochondrial (Gene Name=AADAT)

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