Structure of PDB 1yw0 Chain A Binding Site BS01

Receptor Information

>1yw0 Chain A (length=243) Species: 190485 (Xanthomonas campestris pv. campestris str. ATCC 33913) [Search protein sequence] [Download receptor structure] [Download structure with residue number starting from 1] [View receptor structure]

TYGGYLRLDQLLSAQQPLSEPAHHDEMLFIIQHQTSELWLKLLAHELRAA
IVHLQRDEVWQCRKVLARSKQVLRQLTEQWSVLETLTPSEYMGFRDVLGF
QSLQYRYIEFLLGNKNPQMLQVFAYDPAGQARLREVLEAPSLYEEFLRYL
ARFGHAIPQQYQARDWTAAHVADDTLRPVFERIYENTDRYWREYSLCEDL
VDVETQFQLWRFRHMRTVMRVIGFALALTFFPELFDVRTSVGV

Ligand information

Ligand ID

InChI

InChI=1S/Mg/q+2

InChIKey

JLVVSXFLKOJNIY-UHFFFAOYSA-N

SMILES

Software	SMILES
ACDLabs 10.04 OpenEye OEToolkits 1.5.0	[Mg+2]
CACTVS 3.341	[Mg++]

Formula

Name

MAGNESIUM ION

PDB chain

1yw0 Chain A Residue 401 [Download ligand structure] [Download structure with residue number starting from 1] [View ligand structure]

Receptor-Ligand Complex Structure

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Structure summary

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PDB	1yw0 Crystal structure of the tryptophan 2,3-dioxygenase from Xanthomonas campestris. Northeast Structural Genomics Target XcR13.
Resolution	2.7 Å
Binding residue (original residue number in PDB)	A36 Q37 Q38
Binding residue (residue number reindexed from 1)	A14 Q15 Q16
Annotation score	1

Enzymatic activity

Enzyme Commision number

1.13.11.11: tryptophan 2,3-dioxygenase.

Gene Ontology

	Molecular Function
GO:0004833	tryptophan 2,3-dioxygenase activity
GO:0020037	heme binding
GO:0046872	metal ion binding
GO:0051213	dioxygenase activity

	Biological Process
GO:0006569	tryptophan catabolic process
GO:0019441	tryptophan catabolic process to kynurenine
GO:0019442	tryptophan catabolic process to acetyl-CoA

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Biological Process

External links

PDB	RCSB:1yw0, PDBe:1yw0, PDBj:1yw0
PDBsum	1yw0
PubMed
UniProt	Q8PDA8\|T23O_XANCP Tryptophan 2,3-dioxygenase (Gene Name=kynA)

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