Structure of PDB 3bk9 Chain H

Receptor sequence
>3bk9H (length=257) Species: 340 (Xanthomonas campestris pv. campestris) [Search protein sequence]
LTYGGYLRLDQLLSAQQPLSEPAHHDEMLFIIQAQTSELWLKLLAHELRA
AIVHLQRDEVWQCRKVLARSKQVLRQLTEQWSVLETLTPSEYMGFRDVLG
PSSGFQSLQYRYIEFLLGNKNPQMLQVFAYDPAGQARLREVLEAPSLYEE
FLRYLARFGHAIPQQWTAAHVADDTLRPVFERIYENTDRYWREYSLCEDL
VDVETQFQLWRFRHMRTVMRVIGFKRGTGGSSGVGFLQQALALTFFPELF
DVRTSVG
3D structure
PDB3bk9 Histidine 55 of tryptophan 2,3-dioxygenase is not an active site base but regulates catalysis by controlling substrate binding
ChainH
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 H Y24 Y27 L28 Y3 Y6 L7
BS02 TRP H F51 Y113 R117 L120 S123 G253 T254 F30 Y92 R96 L99 S102 G227 T228
BS03 HEM H S58 W102 S124 G125 F126 Y131 R132 W236 H240 V244 V247 G253 G255 S257 S37 W81 S103 G104 F105 Y110 R111 W210 H214 V218 V221 G227 G229 S231
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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