Structure of PDB 6ud5 Chain A

Receptor sequence

>6ud5A (length=351) Species: 9606 (Homo sapiens)

GLIYGNYLHLEKVLNAQELQSETKGNKIHDEHLFIITHQAYELWFKQILW
ELDSVREIFQNGHVRDERNMLKVVSRMHRVSVILKLLVQQFSILETMTAL
DFNDFREYLSPASGFQSLQFRLLENKIGVLQNMRVPYNRRHYRDNFKGEE
NELLLKSEQEKTLLELVEAWLERTPGLEPHGFNFWGKLEKNITRGLEEEF
IRIQAKEESEEKEEQVAEFQKQKEVLLSLFDEKRHEHLLSKGERRLSYRA
LQGALMIYFYREEPRFQVPFQLLTSLMDIDSLMTKWRYNHVCMVHRMLGS
KAGTGGSSGYHYLRSTVSDRYKVFVDLFNLSTYLIPRHWIPKMNPTIHKF
L

3D structure

• PDB: 6ud5 Conformational Plasticity in Human Heme-Based Dioxygenases.
• Chain: A
• Resolution: 2.05 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	H76 Y79 L132 G152 F153 F158 R159 H328 M331 V332 M335 G341 G343 S345 Y350 L351	H38 Y41 L94 G114 F115 F120 R121 H290 M293 V294 M297 G303 G305 S307 Y312 L313
BS02	TRP	A	F72 H76 R144 L336 G341 T342	F34 H38 R106 L298 G303 T304
BS03	TRP	A	R103 E105 W208 R211 T212 P213 F304 P307	R65 E67 W170 R173 T174 P175 F266 P269

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:6ud5, PDBe:6ud5, PDBj:6ud5
• PDBsum: 6ud5
• PubMed: 33373218
• UniProt: P48775|T23O_HUMAN Tryptophan 2,3-dioxygenase (Gene Name=TDO2)