1doc Summary

pdbe.org/1doc
spacer

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)search. 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):


Chain Name UniProt Name of source organism % of UniProt sequence present in the sample Residues in the sample molecules % of residues observed
A P-HYDROXYBENZOATE HYDROXYLASE P20586 (1-394) (PHHY_PSEAE)search Pseudomonas aeruginosa PAO1search 100% 394 100%


This entry contains 1 unique UniProt protein:

UniProt accession Name Organism PDB
P20586 (1 - 394) P-HYDROXYBENZOATE HYDROXYLASE Pseudomonas aeruginosa

Chain Structural classification (SCOP) Structural classification (CATH) Sequence family (Pfam)
A (P20586) FAD-linked reductases, N-terminal domainsearch, PHBH-likesearch FAD/NAD(P)-binding domainsearch, D-Amino Acid Oxidase, subunit A, domain 2search PF01494: FAD binding domainsearch

Chain ID Molecular function (GO) Biological process (GO)
A (P20586) 4-hydroxybenzoate 3-monooxygenase activitysearch oxidoreductase activitysearch flavin adenine dinucleotide bindingsearch monooxygenase activitysearch benzoate catabolic processsearch oxidation-reduction processsearch metabolic processsearch benzoate catabolic process via hydroxylationsearch aromatic compound catabolic processsearch

Chain InterPro annotation
A Monooxygenase, FAD-bindingsearch Aromatic-ring hydroxylase-likesearch 4-hydroxybenzoate 3-monooxygenasesearch