Structure of PDB 4wlj Chain A Binding Site BS01

Receptor Information
>4wlj Chain A (length=413) Species: 9606 (Homo sapiens) [Search protein sequence] [Download receptor structure] [Download structure with residue number starting from 1] [View receptor structure]
QLQARRLDGIDYNPWVEFVKLASEHDVVNLGQGFPDFPPPDFAVEAFQHA
VSGDFMLNQYTKTFGYPPLTKILASFFGELLGQEIDPLRNVLVTVGGYGA
LFTAFQALVDEGDEVIIIEPFFDCYEPMTMMAGGRPVFVSLKPGLGSSSN
WQLDPMELAGKFTSRTKALVLNTPNNPLGKVFSREELELVASLCQQHDVV
CITDEVYQWMVYDGHQHISIASLPGMWERTLTIGSAGKTFSATGWKVGWV
LGPDHIMKHLRTVHQNSVFHCPTQSQAAVAESFEREQLLFRQPSSYFVQF
PQAMQRCRDHMIRSLQSVGLKPIIPQGSYFLITDISDFKRKMPDLPGAVD
EPYDRRFVKWMIKNKGLVAIPVSIFYSVPHQKHFDHYIRFCFVKDEATLQ
AMDEKLRKWKVEL
Ligand information
Ligand IDIK2
InChIInChI=1S/C10H15N2O8P/c1-6-10(15)8(3-12-19-5-9(13)14)7(2-11-6)4-20-21(16,17)18/h2,12,15H,3-5H2,1H3,(H,13,14)(H2,16,17,18)
InChIKeyQYKRUCBLHROXCK-UHFFFAOYSA-N
SMILES
SoftwareSMILES
CACTVS 3.341Cc1ncc(CO[P](O)(O)=O)c(CNOCC(O)=O)c1O
ACDLabs 10.04O=P(O)(O)OCc1cnc(c(O)c1CNOCC(=O)O)C
OpenEye OEToolkits 1.5.0Cc1c(c(c(cn1)COP(=O)(O)O)CNOCC(=O)O)O
FormulaC10 H15 N2 O8 P
Name4'-DEOXY-4'-ACETYLYAMINO-PYRIDOXAL-5'-PHOSPHATE
ChEMBL
DrugBankDB02783
ZINCZINC000002047479
PDB chain4wlj Chain A Residue 501 [Download ligand structure] [Download structure with residue number starting from 1] [View ligand structure]
Receptor-Ligand Complex Structure
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PDB4wlj High resolution crystal structures of human kynurenine aminotransferase-I bound to PLP cofactor, and in complex with aminooxyacetate.
Resolution1.54 Å
Binding residue
(original residue number in PDB)		W18 G99 G100 Y101 F125 N181 N185 D213 V215 Y216 S244 K247 K255 R398
Binding residue
(residue number reindexed from 1)		W15 G96 G97 Y98 F122 N172 N176 D204 V206 Y207 S235 K238 K246 R389
Annotation score1
Enzymatic activity
Catalytic site (original residue number in PDB) F125 D213 V215 K247
Catalytic site (residue number reindexed from 1) F122 D204 V206 K238
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:4wlj, PDBe:4wlj, PDBj:4wlj
PDBsum4wlj
PubMed28097769
UniProtQ16773|KAT1_HUMAN Kynurenine--oxoglutarate transaminase 1 (Gene Name=KYAT1)

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