Structure of PDB 2nox Chain A Binding Site BS01

Receptor Information
>2nox Chain A (length=261) Species: 119219 (Cupriavidus metallidurans) [Search protein sequence] [Download receptor structure] [Download structure with residue number starting from 1] [View receptor structure]
RDMSYGDYLGLDQILSAQHPLSPDHNEMLFIVQHQTTELWMKLMLHELRA
ARDGVKSDQLQPAFKMLARVSRIMDQLVQAWNVLATMTPPEYSAMRPYLG
ASSGFQSYQYREIEFILGNKNAAMLRPHAHRPEHLELVETALHTPSMYDE
AIRLMARRGFQIDPEVVERDWTQPTQYNASVEAAWLEVYRNPSAHWELYE
LGEKFVDLEDAFRQWRFRHVTTVERVIGFKRGTGGTEGVSYLRRMLDVVL
FPELWKLRTDL
Ligand information
Ligand IDHEM
InChIInChI=1S/C34H34N4O4.Fe/c1-7-21-17(3)25-13-26-19(5)23(9-11-33(39)40)31(37-26)16-32-24(10-12-34(41)42)20(6)28(38-32)15-30-22(8-2)18(4)27(36-30)14-29(21)35-25;/h7-8,13-16H,1-2,9-12H2,3-6H3,(H4,35,36,37,38,39,40,41,42);/q;+2/p-2/b25-13-,26-13-,27-14-,28-15-,29-14-,30-15-,31-16-,32-16-;
InChIKeyKABFMIBPWCXCRK-RGGAHWMASA-L
SMILES
SoftwareSMILES
OpenEye OEToolkits 1.7.6Cc1c2n3c(c1CCC(=O)O)C=C4C(=C(C5=[N]4[Fe]36[N]7=C(C=C8N6C(=C5)C(=C8C)C=C)C(=C(C7=C2)C)C=C)C)CCC(=O)O
CACTVS 3.385CC1=C(CCC(O)=O)C2=Cc3n4[Fe]5|6|N2=C1C=c7n5c(=CC8=N|6C(=Cc4c(C)c3CCC(O)=O)C(=C8C=C)C)c(C)c7C=C
ACDLabs 12.01C=1c3c(c(c4C=C5C(=C(C=6C=C7C(=C(C8=CC=2C(=C(C=1N=2[Fe](n34)(N5=6)N78)CCC(=O)O)C)\C=C)C)\C=C)C)C)CCC(=O)O
FormulaC34 H32 Fe N4 O4
NamePROTOPORPHYRIN IX CONTAINING FE;
HEME
ChEMBL
DrugBankDB18267
ZINC
PDB chain2nox Chain A Residue 500 [Download ligand structure] [Download structure with residue number starting from 1] [View ligand structure]
Receptor-Ligand Complex Structure
Global viewLocal viewStructure summary

[Spin on] [Spin off] [Reset]
[High quality] [Low quality]
[White background] [Black background]
[Spin on] [Spin off] [Reset]
[High quality] [Low quality]
[White background] [Black background]
PDB2nox Crystal structure and mechanism of tryptophan 2,3-dioxygenase, a heme enzyme involved in tryptophan catabolism and in quinolinate biosynthesis.
Resolution2.4 Å
Binding residue
(original residue number in PDB)		F68 H72 T75 W119 L122 Y130 S141 G142 Y148 R149 H257 V261 G270 G272 T274 Y279
Binding residue
(residue number reindexed from 1)		F30 H34 T37 W81 L84 Y92 S103 G104 Y110 R111 H219 V223 G232 G234 T236 Y241
Annotation score1
Enzymatic activity
Enzyme Commision number 1.13.11.11: tryptophan 2,3-dioxygenase.
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

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

[Back to BioLiP]