Structure of PDB 6a4i Chain C

Receptor sequence
>6a4iC (length=323) Species: 9606 (Homo sapiens) [Search protein sequence]
IYGNYLHLEKVLNAQELQSETKGNKIHDEHLFIITHQAYELWFKQILWEL
DSVREIFQNGHVRDERNMLKVVSRMHRVSVILKLLVQQFSILETMTALDF
NDFREYLSPASGFQSLQFRLLENKIGVLQNMRVPYNRRKGEENELLLKSE
QEKTLLELVEAWLERTPGLEPHGFNFWGKLEKNITRGLEEEFIRIQAKEE
QVAEFQKQKEVLLSLFDEKRHEHLLSKGERRLSYRALQGALMIYFYREEP
RFQVPFQLLTSLMDIDSLMTKWRYNHVCMVHRMLGSSGYHYLRSTVSDRY
KVFVDLFNLSTYLIPRHWIPKMN
3D structure
PDB6a4i Crystal Structure of human TDO inhibitor complex
ChainC
Resolution2.65 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 HEM C F72 H76 Y79 L132 F140 S151 G152 F153 F158 R159 Y175 H328 V332 Y350 L351 F32 H36 Y39 L92 F100 S111 G112 F113 F118 R119 Y135 H276 V280 Y291 L292
BS02 9R9 C F72 H76 L147 A150 F32 H36 L107 A110
BS03 9R9 C Y42 Y45 Y2 Y5
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:6a4i, PDBe:6a4i, PDBj:6a4i
PDBsum6a4i
PubMed
UniProtP48775|T23O_HUMAN Tryptophan 2,3-dioxygenase (Gene Name=TDO2)

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