Structure of PDB 2nw8 Chain B

Receptor sequence
>2nw8B (length=264) Species: 340 (Xanthomonas campestris pv. campestris) [Search protein sequence]
RLTYGGYLRLDQLLSAQQPLSEPAHHDEMLFIIQHQTSELWLKLLAHELR
AAIVHLQRDEVWQCRKVLARSKQVLRQLTEQWSVLETLTPSEYMGFRDVL
GPSSGFQSLQYRYIEFLLGNKNPQMLQVFAYDPAGQARLREVLEAPSLYE
EFLRYLARFGHAIPQQYQARDWTAAHVADDTLRPVFERIYENTDRYWREY
SLCEDLVDVETQFQLWRFRHMRTVMRVIGFSSGVGFLQQALALTFFPELF
DVRTSVGVDNRPPQ
3D structure
PDB2nw8 Molecular insights into substrate recognition and catalysis by tryptophan 2,3-dioxygenase.
ChainB
Resolution1.6 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 B F51 G121 S123 F31 G101 S103
BS02 TRP B Y220 S221 E224 D228 Y200 S201 E204 D208
BS03 HEM B H55 S58 W102 L105 S124 G125 F126 Y131 R132 H240 V244 V247 I248 G259 F262 L263 H35 S38 W82 L85 S104 G105 F106 Y111 R112 H220 V224 V227 I228 G233 F236 L237
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:2nw8, PDBe:2nw8, PDBj:2nw8
PDBsum2nw8
PubMed17197414
UniProtQ8PDA8|T23O_XANCP Tryptophan 2,3-dioxygenase (Gene Name=kynA)

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