1foh Summary

pdbe.org/1foh
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PHENOL HYDROXYLASE FROM TRICHOSPORON CUTANEUM

The structure was published by Enroth, C., Neujahr, H., Schneider, G., and Lindqvist, Y., in 1998 in a paper entitled "The crystal structure of phenol hydroxylase in complex with FAD and phenol provides evidence for a concerted conformational change in the enzyme and its cofactor during catalysis." (abstract).

This crystal structure was determined using X-ray diffraction at a resolution of 2.4 Å and deposited in 1998.

The experimental data on which the structure is based was not deposited.

This PDB entry contains multiple copies of the structure of PHENOL HYDROXYLASE.

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 has more than one probable quaternary state observed. For more details see the quaternary structure page.

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 PHENOL HYDROXYLASE P15245 (2-665) (PH2M_TRICU)search Trichosporon cutaneumsearch 100% 664 98%
B PHENOL HYDROXYLASE P15245 (2-665) (PH2M_TRICU)search Trichosporon cutaneumsearch 100% 664 98%
C PHENOL HYDROXYLASE P15245 (2-665) (PH2M_TRICU)search Trichosporon cutaneumsearch 100% 664 98%
D PHENOL HYDROXYLASE P15245 (2-665) (PH2M_TRICU)search Trichosporon cutaneumsearch 100% 664 98%


This entry contains 1 unique UniProt protein:

UniProt accession Name Organism PDB
P15245 (2 - 665) PHENOL HYDROXYLASE Trichosporon cutaneum

Chain Structural classification (SCOP) Structural classification (CATH) Sequence family (Pfam)
A, B, C, D (P15245) FAD-linked reductases, N-terminal domainsearch, Glutathione peroxidase-likesearch, PHBH-likesearch FAD/NAD(P)-binding domainsearch, D-Amino Acid Oxidase, subunit A, domain 2search, Glutaredoxinsearch PF01494: FAD binding domainsearch, PF07976: Phenol hydroxylase, C-terminal dimerisation domainsearch

Chain ID Cellular component (GO) Biological process (GO) Molecular function (GO)
A, B, C, D (P15245) cytoplasmsearch oxidation-reduction processsearch aromatic compound catabolic processsearch phenol-containing compound catabolic processsearch metabolic processsearch monooxygenase activitysearch oxidoreductase activitysearch phenol 2-monooxygenase activitysearch

Chain InterPro annotation
A, B, C, D Monooxygenase, FAD-bindingsearch Aromatic-ring hydroxylase-likesearch Thioredoxin-like foldsearch Phenol hydroxylase, C-terminal dimerisation domainsearch