Structure of PDB 3fvu Chain B Binding Site BS02

Receptor Information
>3fvu Chain B (length=419) Species: 9606 (Homo sapiens) [Search protein sequence] [Download receptor structure] [Download structure with residue number starting from 1] [View receptor structure]
QLQARRLDGIDYNPWVEFVKLASEHDVVNLGQGFPDFPPPDFAVEAFQHA
VSGDFMLNQYTKTFGYPPLTKILASFFGELLGQEIDPLRNVLVTVGGYGA
LFTAFQALVDEGDEVIIIEPFFDCYEPMTMMAGGRPVFVSLKPGPIQNGE
LGSSSNWQLDPMELAGKFTSRTKALVLNTPNNPLGKVFSREELELVASLC
QQHDVVCITDEVYQWMVYDGHQHISIASLPGMWERTLTIGSAGKTFSATG
WKVGWVLGPDHIMKHLRTVHQNSVFHCPTQSQAAVAESFEREQLLFRQPS
SYFVQFPQAMQRCRDHMIRSLQSVGLKPIIPQGSYFLITDISDFKRKMPD
LPGAVDEPYDRRFVKWMIKNKGLVAIPVSIFYSVPHQKHFDHYIRFCFVK
DEATLQAMDEKLRKWKVEL
Ligand information
Ligand IDIAC
InChIInChI=1S/C10H9NO2/c12-10(13)5-7-6-11-9-4-2-1-3-8(7)9/h1-4,6,11H,5H2,(H,12,13)
InChIKeySEOVTRFCIGRIMH-UHFFFAOYSA-N
SMILES
SoftwareSMILES
OpenEye OEToolkits 1.7.6c1ccc2c(c1)c(c[nH]2)CC(=O)O
ACDLabs 12.01O=C(O)Cc2c1ccccc1nc2
CACTVS 3.370OC(=O)Cc1c[nH]c2ccccc12
FormulaC10 H9 N O2
Name1H-INDOL-3-YLACETIC ACID;
INDOLE ACETIC ACID
ChEMBLCHEMBL82411
DrugBankDB07950
ZINCZINC000000083860
PDB chain3fvu Chain B Residue 423 [Download ligand structure] [Download structure with residue number starting from 1] [View ligand structure]
Receptor-Ligand Complex Structure
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PDB3fvu Structural insight into the inhibition of human kynurenine aminotransferase I/glutamine transaminase K
Resolution1.55 Å
Binding residue
(original residue number in PDB)		W18 G36 Y101 F125 R398
Binding residue
(residue number reindexed from 1)		W15 G33 Y98 F122 R395
Annotation score1
Enzymatic activity
Catalytic site (original residue number in PDB) F125 D213 V215 K247
Catalytic site (residue number reindexed from 1) F122 D210 V212 K244
Enzyme Commision number 2.6.1.64: glutamine--phenylpyruvate transaminase.
2.6.1.7: kynurenine--oxoglutarate transaminase.
4.4.1.13: cysteine-S-conjugate beta-lyase.
Gene Ontology
Molecular Function
GO:0005515 protein binding
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:0047316 glutamine-phenylpyruvate transaminase activity
GO:0047804 cysteine-S-conjugate beta-lyase activity
Biological Process
GO:0009058 biosynthetic process
GO:0009617 response to bacterium
GO:0070189 kynurenine metabolic process
GO:0097053 L-kynurenine catabolic process
Cellular Component
GO:0005737 cytoplasm
GO:0005739 mitochondrion
GO:0005829 cytosol

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Molecular Function
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Biological Process
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Cellular Component
External links
PDB RCSB:3fvu, PDBe:3fvu, PDBj:3fvu
PDBsum3fvu
PubMed19338303
UniProtQ16773|KAT1_HUMAN Kynurenine--oxoglutarate transaminase 1 (Gene Name=KYAT1)

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