Structure of PDB 5ti9 Chain B

Receptor sequence

>5ti9B (length=336) Species: 9606 (Homo sapiens)

GGLIYGNYLHLEKVLNAQELQSETKGNKIHDEHLFIITHQAYELWFKQIL
WELDSVREIFQNGHVRDERNMLKVVSRMHRVSVILKLLVQQFSILETMTA
LDFNDFREYLSPASGFQSLQFRLLENKIGVLQNMRRDNFKGEENELLLKS
EQEKTLLELVEAWLERTPGLEPHGFNFWGKLEKNITRGLEEEFIRIQAKE
ESEEKEEQVAEFQKQKEVLLSLFDEKRHEHLLSKGERRLSYRALQGALMI
YFYREEPRFQVPFQLLTSLMDIDSLMTKWRYNHVCMVHRMLGSKAGTGGS
SGYHYLRSTVSDRYKVFVDLFNLSTYLIPRHWIPKM

3D structure

• PDB: 5ti9 Molecular basis for catalysis and substrate-mediated cellular stabilization of human tryptophan 2,3-dioxygenase.
• Chain: B
• Resolution: 2.5 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	TRP	B	Y42 Y45	Y5 Y8
BS02	HEM	B	F72 H76 Y79 L132 G152 F153 F158 R159 W324 H328 M331 V332 G341 G343 S345 L351	F35 H39 Y42 L95 G115 F116 F121 R122 W279 H283 M286 V287 G296 G298 S300 L306
BS03	TRP	B	F72 H76 R144 A150 G341 T342	F35 H39 R107 A113 G296 T297
BS04	TRP	B	R103 E105 W208 R211 T212 P213 F304 P307	R66 E68 W163 R166 T167 P168 F259 P262

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:5ti9, PDBe:5ti9, PDBj:5ti9
• PDBsum: 5ti9
• PubMed: 27762317
• UniProt: P48775|T23O_HUMAN Tryptophan 2,3-dioxygenase (Gene Name=TDO2)