Structure of PDB 2nox Chain K

Receptor sequence
>2noxK (length=255) Species: 119219 (Cupriavidus metallidurans) [Search protein sequence]
RDMSYGDYLGLDQILSAQHPLSPDHNEMLFIVQHQTTELWMKLMLHELRA
ARDGVKSDQLQPAFKMLARVSRIMDQLVQAWNVLATMTPPEYSAMRPYLG
ASSGFQSYQYREIEFILGNKNAAMLRPHAHRPEHLELVETALHTPSMYDE
AIRLMARRGFQIDPEVVERDWTQPTQYNASVEAAWLEVYRNPSAHWELYE
LGEKFVDLEDAFRQWRFRHVTTVERVIGFTEGVSYLRRMLDVVLFPELWK
LRTDL
3D structure
PDB2nox Crystal structure and mechanism of tryptophan 2,3-dioxygenase, a heme enzyme involved in tryptophan catabolism and in quinolinate biosynthesis.
ChainK
Resolution2.4 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 K H72 T75 W119 G142 F143 Y148 H257 V261 G276 Y279 L280 H34 T37 W81 G104 F105 Y110 H219 V223 G232 Y235 L236
Gene Ontology
Molecular Function
GO:0004833 tryptophan 2,3-dioxygenase activity
GO:0020037 heme binding
GO:0042802 identical protein binding
GO:0046872 metal ion binding
GO:0051213 dioxygenase activity
Biological Process
GO:0006569 tryptophan catabolic process
GO:0009435 NAD biosynthetic process
GO:0019441 tryptophan catabolic process to kynurenine
GO:0019442 tryptophan catabolic process to acetyl-CoA
GO:0019805 quinolinate biosynthetic process
Cellular Component
GO:1902494 catalytic complex

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Molecular Function
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Biological Process
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Cellular Component
External links
PDB RCSB:2nox, PDBe:2nox, PDBj:2nox
PDBsum2nox
PubMed17198384
UniProtQ1LK00|T23O_CUPMC Tryptophan 2,3-dioxygenase (Gene Name=kynA)

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