Structure of PDB 2nw7 Chain D

Receptor sequence
>2nw7D (length=260) Species: 340 (Xanthomonas campestris pv. campestris) [Search protein sequence]
RLTYGGYLRLDQLLSAQQPLSEPAHHDEMLFIIQHQTSELWLKLLAHELR
AAIVHLQRDEVWQCRKVLARSKQVLRQLTEQWSVLETLTPSEYMGFRDVL
GPSSGFQSLQYRYIEFLLGNKNPQMLQVFAYDPAGQARLREVLEAPSLYE
EFLRYLARFGHAIPQQYQARDWTAAHVADDTLRPVFERIYENTDRYWREY
SLCEDLVDVETQFQLWRFRHMRTVMRVIGFKRSSGVGFLQQALALTFFPE
LFDVRTSVGV
3D structure
PDB2nw7 Molecular insights into substrate recognition and catalysis by tryptophan 2,3-dioxygenase.
ChainD
Resolution2.7 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 HEM D F51 H55 W102 S124 G125 F126 Y131 H240 V244 F262 L263 F31 H35 W82 S104 G105 F106 Y111 H220 V224 F238 L239
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:2nw7, PDBe:2nw7, PDBj:2nw7
PDBsum2nw7
PubMed17197414
UniProtQ8PDA8|T23O_XANCP Tryptophan 2,3-dioxygenase (Gene Name=kynA)

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