Structure of PDB 3e9k Chain A Binding Site BS02

Receptor Information
>3e9k Chain A (length=446) Species: 9606 (Homo sapiens) [Search protein sequence] [Download receptor structure] [Download structure with residue number starting from 1] [View receptor structure]
LELPADTVQRIAAELKCHPTDERVALHLDEEDKLRHFRECFYIPKIQDLP
PVDLSLVNKDENAIYFLGNSLGLQPKMVKTYLEEELDKWAKIAAYGHEVG
KRPWITGDESIVGLMKDIVGANEKEIALMNALTVNLHLLMLSFFKPTPKR
YKILLEAKAFPSDHYAIESQLQLHGLNIEESMRMIKPREGEETLRIEDIL
EVIEKEGDSIAVILFSGVHFYTGQHFNIPAITKAGQAKGCYVGFDLAHAV
GNVELYLHDWGVDFACWCSYKYLNAGAGGIAGAFIHEKHAHTIKPALVGW
FGHELSTRFKMDNKLQLIPGVCGFRISNPPILLVCSLHASLEIFKQATMK
ALRKKSVLLTGYLEYLIKHNYGVVNIITPSHVEERGCQLTITFSVPNKDV
FQELEKRGVVCDKRNPNGIRVAPVPLYNSFHDVYKFTNLLTSILDS
Ligand information
Ligand ID3XH
InChIInChI=1S/C9H9NO4/c11-7-3-1-2-6(4-7)9(14)10-5-8(12)13/h1-4,11H,5H2,(H,10,14)(H,12,13)
InChIKeyXDOFWFNMYJRHEW-UHFFFAOYSA-N
SMILES
SoftwareSMILES
ACDLabs 10.04O=C(c1cc(O)ccc1)NCC(=O)O
OpenEye OEToolkits 1.5.0c1cc(cc(c1)O)C(=O)NCC(=O)O
CACTVS 3.341OC(=O)CNC(=O)c1cccc(O)c1
FormulaC9 H9 N O4
Name3-Hydroxyhippuric acid;
N-[(3-hydroxyphenyl)carbonyl]glycine
ChEMBLCHEMBL447627
DrugBankDB07069
ZINCZINC000006534965
PDB chain3e9k Chain A Residue 467 [Download ligand structure] [Download structure with residue number starting from 1] [View ligand structure]
Receptor-Ligand Complex Structure
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PDB3e9k Crystal structure of the Homo sapiens kynureninase-3-hydroxyhippuric acid inhibitor complex: insights into the molecular basis of kynureninase substrate specificity.
Resolution1.7 Å
Binding residue
(original residue number in PDB)		S75 F165 H253 K276 R434
Binding residue
(residue number reindexed from 1)		S70 F160 H248 K271 R420
Annotation score1
Binding affinityMOAD: Ki=60uM
BindingDB: Ki=60000nM
Enzymatic activity
Catalytic site (original residue number in PDB) F165 D250 Y275 K276 R434
Catalytic site (residue number reindexed from 1) F160 D245 Y270 K271 R420
Enzyme Commision number 3.7.1.3: kynureninase.
Gene Ontology
Molecular Function
GO:0016787 hydrolase activity
GO:0030170 pyridoxal phosphate binding
GO:0030429 kynureninase activity
GO:0042803 protein homodimerization activity
Biological Process
GO:0006569 tryptophan catabolic process
GO:0009435 NAD biosynthetic process
GO:0019363 pyridine nucleotide biosynthetic process
GO:0019441 tryptophan catabolic process to kynurenine
GO:0019805 quinolinate biosynthetic process
GO:0034341 response to type II interferon
GO:0034354 'de novo' NAD biosynthetic process from tryptophan
GO:0034516 response to vitamin B6
GO:0043420 anthranilate metabolic process
GO:0097053 L-kynurenine catabolic process
Cellular Component
GO:0005654 nucleoplasm
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:3e9k, PDBe:3e9k, PDBj:3e9k
PDBsum3e9k
PubMed19143568
UniProtQ16719|KYNU_HUMAN Kynureninase (Gene Name=KYNU)

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