Structure of PDB 2toh Chain A

Receptor sequence

>2tohA (length=336) Species: 10116 (Rattus norvegicus)

REDKVPWFPRKVSELDKCHHLVTPDLDLDHPGFSDQVYRQRRKLIAEIAF
QYKHGEPIPHVEYTAEEIATWKEVYVTLKGLYATHACREHLEGFQLLERY
CGYREDSIPQLEDVSRFLKERTGFQLRPVAGLLSARDYLASLAFRVFQCT
QYIRHASSPMHSPEPDCCHELLGHVPMLADRTFAQFSQDIGLASLGASDE
EIEKLSTVYWFTVEFGLCKQNGELKAYGAGLLSSYGELLHSLSEEPEVRA
FDPDTAAVQPYQDQTYQPVYFVSESFNDAKDKLRNYASRIQRPFSVKFDP
YTLAIDVLDSPHTIQRSLEGVQDELHTLAHALSAIS

3D structure

• 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.
• Chain: A
• Resolution: 2.3 Å

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.

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	FE	A	H331 H336 E376	H169 H174 E214
BS02	HBI	A	V291 L294 L295 X300 P327 E332 Y371	V129 L132 L133 X138 P165 E170 Y209	MOAD: Ki=70uM PDBbind-CN: -logKd/Ki=4.15,Ki=70uM

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)