TYROSINE PHENOL-LYASE FROM CITROBACTER INTERMEDIUS COMPLEX WITH 3-(4'-HYDROXYPHENYL)PROPIONIC ACID, PYRIDOXAL-5'-PHOSPHATE AND CS+ ION
The structure was published by Sundararaju, B., Antson, A.A., Phillips, R.S., et al., Gollnick, P., Dodson, G.G., and Wilson, K.S., in 1997 in a paper entitled "The crystal structure of Citrobacter freundii tyrosine phenol-lyase complexed with 3-(4'-hydroxyphenyl)propionic acid, together with site-directed mutagenesis and kinetic analysis, demonstrates that arginine 381 is required for substrate specificity." (abstract).
This crystal structure was determined using X-ray diffraction at a resolution of 2.5 Å and deposited in 1997.
The experimental data on which the structure is based was also deposited.
This PDB entry contains multiple copies of the structure of TYROSINE PHENOL-LYASE.
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: