Structure of PDB 3e2t Chain A Binding Site BS02

Receptor Information
>3e2t Chain A (length=307) Species: 9031 (Gallus gallus) [Search protein sequence] [Download receptor structure] [Download structure with residue number starting from 1] [View receptor structure]
NIPWYPKKISDLDKCANRVLMYGSDLDADHPGFKDNVYRKRRKYFADLAM
NYKHGDPIPEIEFTEEEIKTWGTVYRELNKLYPTHACREYLKNLPLLTKY
CGYREDNIPQLEDVSRFLKERTGFTIRPVAGYLSPRDFLAGLAFRVFHCT
QYVRHSSDPLYTPEPDTCHELLGHVPLLAEPSFAQFSQEIGLASLGASDE
AVQKLATCYFFTVEFGLCKQEGQLRVYGAGLLSSISELKHSLSGSAKVKP
FDPKVTCKQECLITTFQEVYFVSESFEEAKEKMREFAKTIKRPFGVKYNP
YTQSVQI
Ligand information
Ligand IDIMD
InChIInChI=1S/C3H4N2/c1-2-5-3-4-1/h1-3H,(H,4,5)/p+1
InChIKeyRAXXELZNTBOGNW-UHFFFAOYSA-O
SMILES
SoftwareSMILES
CACTVS 3.341[nH]1cc[nH+]c1
ACDLabs 10.04c1c[nH+]cn1
OpenEye OEToolkits 1.5.0c1c[nH+]c[nH]1
FormulaC3 H5 N2
NameIMIDAZOLE
ChEMBL
DrugBank
ZINC
PDB chain3e2t Chain A Residue 2 [Download ligand structure] [Download structure with residue number starting from 1] [View ligand structure]
Receptor-Ligand Complex Structure
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PDB3e2t Crystal structure of tryptophan hydroxylase with bound amino acid substrate
Resolution1.9 Å
Binding residue
(original residue number in PDB)		H273 H278 E318
Binding residue
(residue number reindexed from 1)		H169 H174 E214
Annotation score1
Enzymatic activity
Catalytic site (original residue number in PDB) H273 H278 E318 S337
Catalytic site (residue number reindexed from 1) H169 H174 E214 S233
Enzyme Commision number 1.14.16.4: tryptophan 5-monooxygenase.
Gene Ontology
Molecular Function
GO:0004497 monooxygenase activity
GO:0005506 iron ion binding
GO:0016714 oxidoreductase activity, acting on paired donors, with incorporation or reduction of molecular oxygen, reduced pteridine as one donor, and incorporation of one atom of oxygen
Biological Process
GO:0009072 aromatic amino acid metabolic process

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Molecular Function
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Biological Process
External links
PDB RCSB:3e2t, PDBe:3e2t, PDBj:3e2t
PDBsum3e2t
PubMed18937498
UniProtP70080|TPH1_CHICK Tryptophan 5-hydroxylase 1 (Gene Name=TPH1)

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