Structure of PDB 9ezj Chain B

Receptor sequence
>9ezjB (length=319) Species: 9606 (Homo sapiens) [Search protein sequence]
LIYGNYLHLEKVLNAQELQSETKGNKIHDEHLFIITHQAYELWFKQILWE
LDSVREIFQNGHVRDERNMLKVVSRMHRVSVILKLLVQQFSILETMTALD
FNDFREYLSPASGFQSLQFRLLENKIGVLEENELLLKSEQEKTLLELVEA
WLERTPGLEPHGFNFWGKLEKNITRGLEEEFIRIQAKEESEEKEEQVAEF
QKQKEVLLSLFDEKRHEHLLSKGERRLSYRALQGALMIYFYREEPRFQVP
FQLLTSLMDIDSLMTKWRYNHVCMVHRMLGSDRYKVFVDLFNLSTYLIPR
HWIPKMNPTIHKFLYTAEY
3D structure
PDB9ezj Discovery and binding mode of small molecule inhibitors of the apo form of human TDO2
ChainB
Resolution2.612 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 ZIQ B R103 E105 W208 R211 T212 P213 F304 R64 E66 W151 R154 T155 P156 F247
BS02 A1H8G B F72 H76 F129 F140 A150 F153 Q154 S155 H328 F33 H37 F90 F101 A111 F114 Q115 S116 H271
Gene Ontology
Molecular Function
GO:0004833 tryptophan 2,3-dioxygenase activity
GO:0005515 protein binding
GO:0016597 amino acid binding
GO:0019825 oxygen binding
GO:0020037 heme binding
GO:0042802 identical protein binding
GO:0046872 metal ion binding
GO:0051213 dioxygenase activity
Biological Process
GO:0006568 tryptophan metabolic process
GO:0006569 tryptophan catabolic process
GO:0019441 tryptophan catabolic process to kynurenine
GO:0019442 tryptophan catabolic process to acetyl-CoA
GO:0051289 protein homotetramerization
GO:1904842 response to nitroglycerin
Cellular Component
GO:0005829 cytosol

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Cellular Component
External links
PDB RCSB:9ezj, PDBe:9ezj, PDBj:9ezj
PDBsum9ezj
PubMed
UniProtP48775|T23O_HUMAN Tryptophan 2,3-dioxygenase (Gene Name=TDO2)

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