Structure of PDB 2toh Chain A Binding Site BS01

Receptor Information

>2toh Chain A (length=336) Species: 10116 (Rattus norvegicus)

REDKVPWFPRKVSELDKCHHLVTPDLDLDHPGFSDQVYRQRRKLIAEIAF
QYKHGEPIPHVEYTAEEIATWKEVYVTLKGLYATHACREHLEGFQLLERY
CGYREDSIPQLEDVSRFLKERTGFQLRPVAGLLSARDYLASLAFRVFQCT
QYIRHASSPMHSPEPDCCHELLGHVPMLADRTFAQFSQDIGLASLGASDE
EIEKLSTVYWFTVEFGLCKQNGELKAYGAGLLSSYGELLHSLSEEPEVRA
FDPDTAAVQPYQDQTYQPVYFVSESFNDAKDKLRNYASRIQRPFSVKFDP
YTLAIDVLDSPHTIQRSLEGVQDELHTLAHALSAIS

Ligand information

• Ligand ID: FE
• InChI: InChI=1S/Fe/q+3
• InChIKey: VTLYFUHAOXGGBS-UHFFFAOYSA-N
• SMILES:
  ACDLabs 10.04
  CACTVS 3.341
  OpenEye OEToolkits 1.5.0: [Fe+3]
• Formula: Fe
• Name: FE (III) ION
• DrugBank: DB13949
• PDB chain: 2toh Chain A Residue 501

Receptor-Ligand Complex Structure

Structure summary

• PDB: 2toh Crystal structure of tyrosine hydroxylase with bound cofactor analogue and iron at 2.3 A resolution: self-hydroxylation of Phe300 and the pterin-binding site.
• Resolution: 2.3 Å
• Binding residue (original residue number in PDB): H331 H336 E376
• Binding residue (residue number reindexed from 1): H169 H174 E214
• Annotation score: 1

Enzymatic activity

• Catalytic site (original residue number in PDB): H331 H336 E376 S395
• Catalytic site (residue number reindexed from 1): H169 H174 E214 S233
• 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

External links

• PDB: RCSB:2toh, PDBe:2toh, PDBj:2toh
• PDBsum: 2toh
• PubMed: 9753429
• UniProt: P04177|TY3H_RAT Tyrosine 3-monooxygenase (Gene Name=Th)