Structure of PDB 2nw9 Chain B

Receptor sequence
>2nw9B (length=269) Species: 340 (Xanthomonas campestris pv. campestris) [Search protein sequence]
DLEGRLTYGGYLRLDQLLSAQQPLSEPAHHDEMLFIIQHQTSELWLKLLA
HELRAAIVHLQRDEVWQCRKVLARSKQVLRQLTEQWSVLETLTPSEYMGF
RDVLGPSSGFQSLQYRYIEFLLGNKNPQMLQVFAYDPAGQARLREVLEAP
SLYEEFLRYLARFGHAIPQQYQARDWTAAHVADDTLRPVFERIYENTDRY
WREYSLCEDLVDVETQFQLWRFRHMRTVMRVIGFSSGVGFLQQALALTFF
PELFDVRTSVGVDNRPPQG
3D structure
PDB2nw9 Molecular insights into substrate recognition and catalysis by tryptophan 2,3-dioxygenase.
ChainB
Resolution1.8 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 FT6 B Y24 L28 Y8 L12
BS02 HEM B H55 S58 W102 L105 S124 G125 F126 Y131 H240 V244 V247 I248 G259 F262 L263 H39 S42 W86 L89 S108 G109 F110 Y115 H224 V228 V231 I232 G237 F240 L241
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:2nw9, PDBe:2nw9, PDBj:2nw9
PDBsum2nw9
PubMed17197414
UniProtQ8PDA8|T23O_XANCP Tryptophan 2,3-dioxygenase (Gene Name=kynA)

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