Structure of PDB 5tia Chain A

Receptor sequence

>5tiaA (length=337) Species: 9606 (Homo sapiens)

GLIYGNYLHLEKVLNAQELQSETKGNKIHDEHLFIITHQAYELWFKQILW
ELDSVREIFQNGHVRDERNMLKVVSRMHRVSVILKLLVQQFSILETMTAL
DFNDFREYLSPASGFQSLQFRLLENKIGVLQNMRVPYNRRHYRDNFKGEE
NELLLKSEQEKTLLELVEAWLERTPGLEPHGFNFWGKLEKNITRGLEEEF
IRIQAKEEQVAEFQKQKEVLLSLFDEKRHEHLLSKGERRLSYRALQGALM
IYFYREEPRFQVPFQLLTSLMDIDSLMTKWRYNHVCMVHRMLGSKAGTGG
SSGYHYLRSTVSDRYKVFVDLFNLSTYLIPRHWIPKM

3D structure

• PDB: 5tia Molecular basis for catalysis and substrate-mediated cellular stabilization of human tryptophan 2,3-dioxygenase.
• Chain: A
• Resolution: 2.441 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	HEM	A	F72 H76 Y79 F140 S151 G152 F153 F158 R159 H328 M331 V332 M335 G341 G343 S345 L351	F34 H38 Y41 F102 S113 G114 F115 F120 R121 H284 M287 V288 M291 G297 G299 S301 L307
BS02	TRP	A	F72 H76 R144 A150 S151 L336 G341 T342	F34 H38 R106 A112 S113 L292 G297 T298
BS03	TRP	A	R103 E105 W208 R211 P213 F304	R65 E67 W170 R173 P175 F260

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