2toh Summary



The structure was published by Goodwill, K.E., Sabatier, C., and Stevens, R.C., in 1998 in a paper entitled "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." (abstract).

This crystal structure was determined using X-ray diffraction at a resolution of 2.3 Å and deposited in 1998.

The experimental data on which the structure is based was also deposited.

The PDB entry contains the structure of TYROSINE 3-MONOOXYGENASE. This molecule has the UniProt identifier P04177 (TY3H_RAT)search. The sample contained 343 residues which is < 90% of the natural sequence. Out of 343 residues 336 were observed and are deposited in the PDB.

It also contains one or more heterogenic compounds (e.g., ligands, co-factors, ions, modified amino acids, etc.); see here for a complete list.

The molecule most likely forms homotetramers.

The following tables show cross-reference information to other databases (to obtain a list of all PDB entries sharing the same property or classification, click on the magnifying glass icon):

Chain Name UniProt Name of source organism % of UniProt sequence present in the sample Residues in the sample molecules % of residues observed
A TYROSINE 3-MONOOXYGENASE P04177 (156-498) (TY3H_RAT)search Rattus norvegicussearch < 90% 343 97%

This entry contains 1 unique UniProt protein:

UniProt accession Name Organism PDB
P04177 (156 - 498) TYROSINE 3-MONOOXYGENASE Rattus norvegicus

Chain Structural classification (SCOP) Structural classification (CATH) Sequence family (Pfam)
A Aromatic aminoacid monoxygenases, catalytic and oligomerization domainssearch Phenylalanine Hydroxylasesearch Biopterin-dependent aromatic amino acid hydroxylasesearch

Chain ID Molecular function (GO) Biological process (GO)
A (P04177) monooxygenase activitysearch iron ion bindingsearch oxidoreductase activity, acting on paired donors, with incorporation or reduction of molecular oxygen, reduced pteridine as one donor, and incorporation of one atom of oxygensearch aromatic amino acid family metabolic processsearch oxidation-reduction processsearch

Chain InterPro annotation
A Aromatic amino acid hydroxylasesearch Aromatic amino acid hydroxylase, iron/copper binding sitesearch Aromatic amino acid hydroxylase, C-terminalsearch