Structure of PDB 4hka Chain A

Receptor sequence
>4hkaA (length=345) Species: 7227 (Drosophila melanogaster) [Search protein sequence]
GKIYGEYLMLDKLLDAQCMLSEEDKRPVHDEHLFIITHQAYELWFKQIIF
EFDSIRDMLDAEVIDETKTLEIVKRLNRVVLILKLLVDQVPILETMTPLD
FMDFRKYLAPASGFQSLQFRLIENKLGVLTEQRVRYNQKYSDVFSDEEAR
NSIRNSEKDPSLLELVQRWLERTPGLEESGFNFWAKFQESVDRFLEAQVQ
SAMEEPVEKAKNYRLMDIEKRREVYRSIFDPAVHDALVRRGDRRFSHRAL
QGAIMITFYRDEPRFSQPHQLLTLLMDIDSLITKWRYNHVIMVQRMIGSQ
QLGTGGSSGYQYLRSTLSDRYKVFLDLFNLSTFLIPREAIPPLDE
3D structure
PDB4hka Crystal structure of Drosophila melanogaster tryptophan 2,3-dioxygenase reveals insights into substrate recognition and catalytic mechanism.
ChainA
Resolution2.7 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 H61 Y64 F68 L116 F124 F137 Q138 F142 Y159 W308 H312 V316 Y335 L336 H38 Y41 F45 L93 F101 F114 Q115 F119 Y136 W285 H289 V293 Y312 L313
Gene Ontology
Molecular Function
GO:0004833 tryptophan 2,3-dioxygenase activity
GO:0020037 heme binding
GO:0046872 metal ion binding
GO:0051213 dioxygenase activity
Biological Process
GO:0006569 tryptophan catabolic process
GO:0006727 ommochrome biosynthetic process
GO:0019441 tryptophan catabolic process to kynurenine
GO:0019442 tryptophan catabolic process to acetyl-CoA
GO:0048072 compound eye pigmentation
GO:0051289 protein homotetramerization
GO:0070189 kynurenine metabolic process
Cellular Component
GO:0005575 cellular_component

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Molecular Function
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Cellular Component
External links
PDB RCSB:4hka, PDBe:4hka, PDBj:4hka
PDBsum4hka
PubMed23333332
UniProtP20351|T23O_DROME Tryptophan 2,3-dioxygenase (Gene Name=v)

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