Brand  (β version)

  The number of atoms exceeds 100,000.
  So, it can not be displayed here.

Select unit:

Select hetatm:   

close
information
centroid:
interaction residue:

Select chain:   Sequence  

Data format:   

Color scheme of protein:

Ligands
Code Name Style Show Link
CL Chloride ion
FAD Flavin-adenine dinucleotide
IPH Phenol
Non-standard Residues
Code Name Show
Glycosylation
Code Name Emphasize
Modification
Code Name Show
Code : 1PN0   PDBj   RCSB PDB   PDBe
Header : OXIDOREDUCTASE
Title : Phenol hydroxylase from Trichosporon cutaneum
Release Data : 2003-09-23
Compound :
mol_id molecule chains synonym
1 Phenol 2-monooxygenase A,B,C,D Phenol hydroxylase
ec: 1.14.13.7
Source :
mol_id organism_scientific expression_system
1 Trichosporon cutaneum  (taxid:5554) Escherichia coli  (taxid:562)
Authors : Enroth, C.
Keywords : two dimers, TLS refinement, OXIDOREDUCTASE
Exp. method : X-RAY DIFFRACTION ( 1.70 Å )
Citation :

High-resolution structure of phenol hydroxylase and correction of sequence errors.

Enroth, C.
(2003)  Acta Crystallogr.,Sect.D  59 : 1597 - 1602

PubMed: 12925790
DOI: 10.1107/S0907444903014902

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

Enroth, C.,Neujahr, H.,Schneider, G.  et al.
(1998)  Structure  6 : 605 - 617

DOI: 10.1016/S0969-2126(98)00062-8

Chain : A, B, C, D
UniProt : P15245 (PHHY_CUTCT)
Reaction: EC: Evidence:
Physiological Direction:
H(+) + NADPH + O2 + phenol = catechol + H2O + NADP(+) 1.14.13.7 PubMed:11591156, PubMed:1429434, PubMed:17425111, PubMed:2022646, PubMed:3203745, PubMed:4146224, PubMed:7851397, PubMed:7858421
-