Structure of PDB 6vbn Chain A

Receptor sequence
>6vbnA (length=344) Species: 9606 (Homo sapiens) [Search protein sequence]
LIYGNYLHLEKVLNAQELQSETKGNKIHDEHLFIITHQAYELWFKQILWE
LDSVREIFQNGHVRDERNMLKVVSRMHRVSVILKLLVQQFSILETMTALD
FNDFREYLSPASGFQSLQFRLLENKIGVLQNMRVPYNRRHYRDNFKGEEN
ELLLKSEQEKTLLELVEAWLERTPGLEPHGFNFWGKLEKNITRGLEEEFI
RIQAKEESEEKEEQVAEFQKQKEVLLSLFDEKRHEHLLSKGERRLSYRAL
QGALMIYFYREEPRFQVPFQLLTSLMDIDSLMTKWRYNHVCMVHRMLGSK
AGTGGSSGYHYLRSTVSDRYKVFVDLFNLSTYLIPRHWIPKMNP
3D structure
PDB6vbn Implementation of the CYP Index for the Design of Selective Tryptophan-2,3-dioxygenase Inhibitors.
ChainA
Resolution3.18 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 A H76 Y79 L132 F140 S151 G152 F153 F158 R159 W324 H328 V332 M335 L336 Y350 L351 H37 Y40 L93 F101 S112 G113 F114 F119 R120 W285 H289 V293 M296 L297 Y311 L312
BS02 QVY A F72 H76 L147 A150 G152 F33 H37 L108 A111 G113 BindingDB: EC50=72nM
BS03 QVY A Y42 Y45 Y3 Y6 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

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Molecular Function
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Biological Process
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Cellular Component
External links
PDB RCSB:6vbn, PDBe:6vbn, PDBj:6vbn
PDBsum6vbn
PubMed32292562
UniProtP48775|T23O_HUMAN Tryptophan 2,3-dioxygenase (Gene Name=TDO2)

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