Structure of PDB 1toh Chain A Binding Site BS01

Receptor Information
>1toh Chain A (length=325) Species: 10116 (Rattus norvegicus) [Search protein sequence] [Download receptor structure] [Download structure with residue number starting from 1] [View receptor structure]
KVPWFPRKVSELDKCDLDHPGFSDQVYRQRRKLIAEIAFQYKHGEPIPHV
EYTAEEIATWKEVYVTLKGLYATHACREHLEGFQLLERYCGYREDSIPQL
EDVSRFLKERTGFQLRPVAGLLSARDFLASLAFRVFQCTQYIRHASSPMH
SPEPDCCHELLGHVPMLADRTFAQFSQDIGLASLGASDEEIEKLSTVYWF
TVEFGLCKQNGELKAYGAGLLSSYGELLHSLSEEPEVRAFDPDTAAVQPY
QDQTYQPVYFVSESFNDAKDKLRNYASRIQRPFSVKFDPYTLAIDVLDSP
HTIQRSLEGVQDELHTLAHALSAIS
Ligand information
Ligand IDFE
InChIInChI=1S/Fe/q+3
InChIKeyVTLYFUHAOXGGBS-UHFFFAOYSA-N
SMILES
SoftwareSMILES
ACDLabs 10.04
CACTVS 3.341
OpenEye OEToolkits 1.5.0		[Fe+3]
FormulaFe
NameFE (III) ION
ChEMBL
DrugBankDB13949
ZINC
PDB chain1toh Chain A Residue 501 [Download ligand structure] [Download structure with residue number starting from 1] [View ligand structure]
Receptor-Ligand Complex Structure
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PDB1toh Crystal structure of tyrosine hydroxylase at 2.3 A and its implications for inherited neurodegenerative diseases.
Resolution2.3 Å
Binding residue
(original residue number in PDB)		H331 H336 E376
Binding residue
(residue number reindexed from 1)		H158 H163 E203
Annotation score1
Enzymatic activity
Catalytic site (original residue number in PDB) H331 H336 E376 S395
Catalytic site (residue number reindexed from 1) H158 H163 E203 S222
Enzyme Commision number 1.14.16.2: tyrosine 3-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:1toh, PDBe:1toh, PDBj:1toh
PDBsum1toh
PubMed9228951
UniProtP04177|TY3H_RAT Tyrosine 3-monooxygenase (Gene Name=Th)

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