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4HKA

Crystal structure of Drosophila melanogaster tryptophan 2,3-dioxygenase in complex with HEME

Functional Information from GO Data
ChainGOidnamespacecontents
A0004833molecular_functiontryptophan 2,3-dioxygenase activity
A0005575cellular_componentcellular_component
A0006569biological_processtryptophan catabolic process
A0006727biological_processommochrome biosynthetic process
A0019441biological_processtryptophan catabolic process to kynurenine
A0019442biological_processtryptophan catabolic process to acetyl-CoA
A0020037molecular_functionheme binding
A0046872molecular_functionmetal ion binding
A0048072biological_processcompound eye pigmentation
A0051213molecular_functiondioxygenase activity
A0051289biological_processprotein homotetramerization
A0070189biological_processkynurenine metabolic process
Functional Information from PDB Data
site_idAC1
Number of Residues22
DetailsBINDING SITE FOR RESIDUE HEM A 401
ChainResidue
ATYR27
AGLN138
APHE142
ATYR159
AASN160
ATRP308
AARG309
AHIS312
AMET315
AVAL316
AMET319
APHE57
ATYR335
ALEU336
AHOH521
AHIS61
ATYR64
APHE68
ALEU116
APHE124
AALA134
APHE137

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues3
DetailsBINDING: BINDING => ECO:0000255|HAMAP-Rule:MF_03020
ChainResidueDetails
APHE57
AARG128
ATHR327

site_idSWS_FT_FI2
Number of Residues1
DetailsBINDING: axial binding residue => ECO:0000255|HAMAP-Rule:MF_03020, ECO:0000269|PubMed:23333332, ECO:0007744|PDB:4HKA
ChainResidueDetails
AHIS312

223166

PDB entries from 2024-07-31

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