Structure of PDB 3e08 Chain E

Receptor sequence
>3e08E (length=278) Species: 340 (Xanthomonas campestris pv. campestris) [Search protein sequence]
LRDLEPGIHTDLEGRLTYGGYLRLDQLLSAQQPLSEPAHHDEMLFIIQSQ
TSELWLKLLAHELRAAIVHLQRDEVWQCRKVLARSKQVLRQLTEQWSVLE
TLTPSEYMGFRDVLGPSSGFQSLQYRYIEFLLGNKNPQMLQVFAYDPAGQ
ARLREVLEAPSLYEEFLRYLARFGHAIPQQYQARDWTAAHVADDTLRPVF
ERIYENTDRYWREYSLCEDLVDVETQFQLWRFRHMRTVMRVIGFKRGTGG
SSGVGFLQQALALTFFPELFDVRTSVGV
3D structure
PDB3e08 Histidine 55 of tryptophan 2,3-dioxygenase is not an active site base but regulates catalysis by controlling substrate binding
ChainE
Resolution1.9 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 E F51 Y113 R117 L120 S123 G253 T254 F45 Y107 R111 L114 S117 G247 T248
BS02 HEM E S58 W102 S124 G125 F126 Y131 H240 V244 V247 G253 G255 S257 L263 S52 W96 S118 G119 F120 Y125 H234 V238 V241 G247 G249 S251 L257
BS03 TRP E Y220 S221 E224 D228 Y214 S215 E218 D222
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:3e08, PDBe:3e08, PDBj:3e08
PDBsum3e08
PubMed18783250
UniProtQ8PDA8|T23O_XANCP Tryptophan 2,3-dioxygenase (Gene Name=kynA)

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