THE MOBIL FLAVIN OF 4-OH BENZOATE HYDROXYLASE: MOTION OF A PROSTHETIC GROUP REGULATES CATALYSIS
The structure was published by Gatti, D.L., Palfey, B.A., Lah, M.S., et al., Massey, V., Ballou, D.P., and Ludwig, M.L., in 1994 in a paper entitled "The mobile flavin of 4-OH benzoate hydroxylase." (abstract).
This crystal structure was determined using X-ray diffraction at a resolution of 2.0 Å and deposited in 1994.
The experimental data on which the structure is based was not deposited.
The PDB entry contains the structure of P-HYDROXYBENZOATE HYDROXYLASE. This molecule has the UniProt identifier P20586 (PHHY_PSEAE). The sample contained 394 residues which is 100% of the natural sequence. Out of 394 residues 394 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 homodimers.
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: