Structure of PDB 3bk9 Chain E

Receptor sequence
>3bk9E (length=260) Species: 340 (Xanthomonas campestris pv. campestris) [Search protein sequence]
TYGGYLRLDQLLSAQQPLSEPAHHDEMLFIIQAQTSELWLKLLAHELRAA
IVHLQRDEVWQCRKVLARSKQVLRQLTEQWSVLETLTPSEYMGFRDVLGP
SSGFQSLQYRYIEFLLGNKNPQMLQVFAYDPAGQARLREVLEAPSLYEEF
LRYLARFGHAIPQQYQARDWTAAHVADDTLRPVFERIYENTDRYWREYSL
CEDLVDVETQFQLWRFRHMRTVMRVIGFKRGTGGSSGVGFLQQALALTFF
PELFDVRTSV
3D structure
PDB3bk9 Histidine 55 of tryptophan 2,3-dioxygenase is not an active site base but regulates catalysis by controlling substrate binding
ChainE
Resolution2.15 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 S123 T254 F29 Y91 R95 S101 T232
BS02 HEM E F51 S58 W102 L105 S124 G125 F126 Y131 R132 H240 V244 G253 G255 S257 L263 F29 S36 W80 L83 S102 G103 F104 Y109 R110 H218 V222 G231 G233 S235 L241
BS03 TRP E R85 S221 D228 R63 S199 D206
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:3bk9, PDBe:3bk9, PDBj:3bk9
PDBsum3bk9
PubMed18783250
UniProtQ8PDA8|T23O_XANCP Tryptophan 2,3-dioxygenase (Gene Name=kynA)

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