PDBsum entry 1pn0

Oxidoreductase

PDB id: 1pn0

Contents

Protein chains

652 a.a. *

Ligands

FAD ×4

IPH ×4

Metals

_CL ×4

Waters ×2688

* Residue conservation analysis

PDB id:

1pn0

Name:

Oxidoreductase

Title:

Phenol hydroxylase from trichosporon cutaneum

Structure:

Phenol 2-monooxygenase. Chain: a, b, c, d. Synonym: phenol hydroxylase. Engineered: yes

Source:

Trichosporon cutaneum. Organism_taxid: 5554. Expressed in: escherichia coli. Expression_system_taxid: 562

Biol. unit:

Dimer (from PQS)

Resolution:

1.70Å R-factor: 0.157 R-free: 0.180

Authors:

C.Enroth

Key ref:

C.Enroth (2003). High-resolution structure of phenol hydroxylase and correction of sequence errors. Acta Crystallogr D Biol Crystallogr, 59, 1597-1602. PubMed id: 12925790 DOI: 10.1107/S0907444903014902

Date:

12-Jun-03 Release date: 23-Sep-03

Protein chains

P15245  (PHHY_CUTCT) -  Phenol hydroxylase from Cutaneotrichosporon cutaneum

Seq: 665 a.a.

Struc: 652 a.a.*

* PDB and UniProt seqs differ at 12 residue positions (black crosses)

Enzyme reactions

• Enzyme class: E.C.1.14.13.7 - phenol 2-monooxygenase (NADPH).
• Reaction: phenol + NADPH + O2 + H⁺ = catechol + NADP⁺ + H2O

phenol + NADPH + O2 + H(+) (Bound ligand (Het Group name = IPH) corresponds exactly) = catechol + NADP(+) + H2O

• Cofactor: FAD

FAD (Bound ligand (Het Group name = FAD) corresponds exactly)

Molecule diagrams generated from .mol files obtained from the KEGG ftp site

reference

DOI no: 10.1107/S0907444903014902

Acta Crystallogr D Biol Crystallogr 59:1597-1602 (2003)

PubMed id: 12925790

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

C.Enroth.

ABSTRACT

The crystal structure model of phenol hydroxylase has been corrected for 11 sequence errors and refined against new data to 1.7 A resolution. The higher resolution data together with careful exploitation of non-crystallographic symmetry restraints and the use of many small groups for refinement of anisotropic displacement parameters resulted in a large decrease in the crystallographic R factor. The final crystallographic free R factor is 18.0%, which should be compared with the values of 27.8% for the previously published model (PDB code 1foh). The rebuilding and re-refinement procedure is described. A comparison with the previously published model was performed and possible biochemical implications are discussed. No large differences suggesting gross errors in the earlier model were found. The actual differences between these two models give an indication of the level of ambiguity and inaccuracy that may be found in a well refined protein model at 2.4 A resolution.

Selected figure(s)

Figure 2.
Figure 2 A figure showing the eight structural domains of a subunit which were treated as independent domains in the TLS refinement. FAD, which was treated as another separate TLS domain, is shown in ball-and-stick representation. This figure was prepared with MOLSCRIPT (Kraulis, 1991[Kraulis, P. J. (1991). J. Appl. Cryst. 24, 946-950.]) and Raster3D (Merritt & Murphy, 1994[Merritt, E. A. & Murphy, M. E. P. (1994). Acta Cryst. D50, 869-873.]).

The above figure is reprinted by permission from the IUCr: Acta Crystallogr D Biol Crystallogr (2003, 59, 1597-1602) copyright 2003.

Figure was selected by an automated process.