Structure of PDB 2nw9 Chain A

Receptor sequence
>2nw9A (length=265) Species: 340 (Xanthomonas campestris pv. campestris) [Search protein sequence]
GRLTYGGYLRLDQLLSAQQPLSEPAHHDEMLFIIQHQTSELWLKLLAHEL
RAAIVHLQRDEVWQCRKVLARSKQVLRQLTEQWSVLETLTPSEYMGFRDV
LGPSSGFQSLQYRYIEFLLGNKNPQMLQVFAYDPAGQARLREVLEAPSLY
EEFLRYLARFGHAIPQQYQARDWTAAHVADDTLRPVFERIYENTDRYWRE
YSLCEDLVDVETQFQLWRFRHMRTVMRVIGFKRGTGGSSGVGFLQQALAL
TFFPELFDVRTSVGV
3D structure
PDB2nw9 Molecular insights into substrate recognition and catalysis by tryptophan 2,3-dioxygenase.
ChainA
Resolution1.8 Å
3D
structure
[Spin on]
[Spin off]
[Reset orientation]

[High quality]
[Low quality]

[White background]
[Black background]

[Download]
[Download structure with residue number starting from 1]
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 A F51 H55 Y113 R117 L120 S123 G253 T254 F32 H36 Y94 R98 L101 S104 G234 T235
BS02 HEM A F51 H55 S58 W102 L105 G125 F126 Y131 R132 H240 V244 I248 G253 G255 S257 F32 H36 S39 W83 L86 G106 F107 Y112 R113 H221 V225 I229 G234 G236 S238
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

View graph for
Molecular Function
View graph for
Biological Process
External links
PDB RCSB:2nw9, PDBe:2nw9, PDBj:2nw9
PDBsum2nw9
PubMed17197414
UniProtQ8PDA8|T23O_XANCP Tryptophan 2,3-dioxygenase (Gene Name=kynA)

[Back to BioLiP]