TYROSINE HYDROXYLASE CATALYTIC AND TETRAMERIZATION DOMAINS FROM RAT
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). 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):
This entry contains 1 unique UniProt protein: