Structure of PDB 6vbn Chain B

Receptor sequence

>6vbnB (length=343) Species: 9606 (Homo sapiens)

LIYGNYLHLEKVLNAQELQSETKGNKIHDEHLFIITHQAYELWFKQILWE
LDSVREIFQNGHVRDERNMLKVVSRMHRVSVILKLLVQQFSILETMTALD
FNDFREYLSPASGFQSLQFRLLENKIGVLQNMRVPYNRRHYRDNFKGEEN
ELLLKSEQEKTLLELVEAWLERTPGLEPHGFNFWGKLEKNITRGLEEEFI
RIQAKEESEEKEEQVAEFQKQKEVLLSLFDEKRHEHLLSKGERRLSYRAL
QGALMIYFYREEPRFQVPFQLLTSLMDIDSLMTKWRYNHVCMVHRMLGSK
AGTGGSSGYHYLRSTVSDRYKVFVDLFNLSTYLIPRHWIPKMN

3D structure

• PDB: 6vbn Implementation of the CYP Index for the Design of Selective Tryptophan-2,3-dioxygenase Inhibitors.
• Chain: B
• Resolution: 3.18 Å

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	QVY	B	Y42 Y45	Y3 Y6	BindingDB: EC50=72nM
BS02	HEM	B	H76 Y79 L132 S151 G152 F153 F158 R159 W324 H328 V332 M335 Y350 L351	H37 Y40 L93 S112 G113 F114 F119 R120 W285 H289 V293 M296 Y311 L312
BS03	QVY	B	F72 H76 A150 G152	F33 H37 A111 G113	BindingDB: EC50=72nM

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

External links

• PDB: RCSB:6vbn, PDBe:6vbn, PDBj:6vbn
• PDBsum: 6vbn
• PubMed: 32292562
• UniProt: P48775|T23O_HUMAN Tryptophan 2,3-dioxygenase (Gene Name=TDO2)