Structure of PDB 2nw8 Chain A

Receptor sequence
>2nw8A (length=266) Species: 340 (Xanthomonas campestris pv. campestris) [Search protein sequence]
EGRLTYGGYLRLDQLLSAQQPLSEPAHHDEMLFIIQHQTSELWLKLLAHE
LRAAIVHLQRDEVWQCRKVLARSKQVLRQLTEQWSVLETLTPSEYMGFRD
VLGPSSGFQSLQYRYIEFLLGNKNPQMLQVFAYDPAGQARLREVLEAPSL
YEEFLRYLARFGHAIPQQYQARDWTAAHVADDTLRPVFERIYENTDRYWR
EYSLCEDLVDVETQFQLWRFRHMRTVMRVIGFKRGTGGSSGVGFLQQALA
LTFFPELFDVRTSVGV
3D structure
PDB2nw8 Molecular insights into substrate recognition and catalysis by tryptophan 2,3-dioxygenase.
ChainA
Resolution1.6 Å
3D
structure
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Enzymatic activity
Enzyme Commision number 1.13.11.11: tryptophan 2,3-dioxygenase.
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 TRP A F51 H55 Y113 R117 S123 G253 T254 F33 H37 Y95 R99 S105 G235 T236
BS02 TRP A Y220 S221 E224 D228 Y202 S203 E206 D210
BS03 HEM A F51 H55 S58 W102 Y113 G125 F126 Y131 R132 H240 V244 G253 G255 S257 F33 H37 S40 W84 Y95 G107 F108 Y113 R114 H222 V226 G235 G237 S239
BS04 TRP A Y24 Y27 Y6 Y9
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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Molecular Function
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Biological Process
External links
PDB RCSB:2nw8, PDBe:2nw8, PDBj:2nw8
PDBsum2nw8
PubMed17197414
UniProtQ8PDA8|T23O_XANCP Tryptophan 2,3-dioxygenase (Gene Name=kynA)

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