Structure of PDB 2nox Chain A

Receptor sequence
>2noxA (length=261) Species: 119219 (Cupriavidus metallidurans) [Search protein sequence]
RDMSYGDYLGLDQILSAQHPLSPDHNEMLFIVQHQTTELWMKLMLHELRA
ARDGVKSDQLQPAFKMLARVSRIMDQLVQAWNVLATMTPPEYSAMRPYLG
ASSGFQSYQYREIEFILGNKNAAMLRPHAHRPEHLELVETALHTPSMYDE
AIRLMARRGFQIDPEVVERDWTQPTQYNASVEAAWLEVYRNPSAHWELYE
LGEKFVDLEDAFRQWRFRHVTTVERVIGFKRGTGGTEGVSYLRRMLDVVL
FPELWKLRTDL
3D structure
PDB2nox Crystal structure and mechanism of tryptophan 2,3-dioxygenase, a heme enzyme involved in tryptophan catabolism and in quinolinate biosynthesis.
ChainA
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 A F68 H72 T75 W119 L122 Y130 S141 G142 Y148 R149 H257 V261 G270 G272 T274 Y279 F30 H34 T37 W81 L84 Y92 S103 G104 Y110 R111 H219 V223 G232 G234 T236 Y241
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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