Structure of PDB 3e08 Chain H

Receptor sequence
>3e08H (length=276) Species: 340 (Xanthomonas campestris pv. campestris) [Search protein sequence]
LRDLEPGIHTDLEGRLTYGGYLRLDQLLSAQQPLSEPAHHDEMLFIIQSQ
TSELWLKLLAHELRAAIVHLQRDEVWQCRKVLARSKQVLRQLTEQWSVLE
TLTPSEYMGFRDVLGPSSGFQSLQYRYIEFLLGNKNPQMLQVFAYDPAGQ
ARLREVLEAPSLYEEFLRYLARFGHAIPQQYQARDWTAAHVADDTLRPVF
ERIYENTDRYWREYSLCEDLVDVETQFQLWRFRHMRTVMRVIGFKRGTGG
SSGVGFLQQALALTFFPELFDVRTSV
3D structure
PDB3e08 Histidine 55 of tryptophan 2,3-dioxygenase is not an active site base but regulates catalysis by controlling substrate binding
ChainH
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 H Y24 Y27 Y18 Y21
BS02 TRP H Y220 S221 E224 D228 Y214 S215 E218 D222
BS03 TRP H F51 Y113 R117 S123 G253 T254 F45 Y107 R111 S117 G247 T248
BS04 HEM H W102 S124 G125 F126 Y131 R132 H240 V244 V247 I248 G253 G255 S257 L263 W96 S118 G119 F120 Y125 R126 H234 V238 V241 I242 G247 G249 S251 L257
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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