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Chlorine in PDB 1wvf: P-Cresol Methylhydroxylase: Alteration of the Structure of the Flavoprotein Subunit Upon Its Binding to the Cytochrome Subunit

Enzymatic activity of P-Cresol Methylhydroxylase: Alteration of the Structure of the Flavoprotein Subunit Upon Its Binding to the Cytochrome Subunit

All present enzymatic activity of P-Cresol Methylhydroxylase: Alteration of the Structure of the Flavoprotein Subunit Upon Its Binding to the Cytochrome Subunit:
1.17.99.1;

Protein crystallography data

The structure of P-Cresol Methylhydroxylase: Alteration of the Structure of the Flavoprotein Subunit Upon Its Binding to the Cytochrome Subunit, PDB code: 1wvf was solved by L.M.Cunane, Z.-W.Chen, W.S.Mcintire, F.S.Mathews, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 30.00 / 1.30
Space group C 1 2 1
Cell size a, b, c (Å), α, β, γ (°) 88.640, 116.910, 50.220, 90.00, 113.18, 90.00
R / Rfree (%) 14.6 / 16.7

Chlorine Binding Sites:

The binding sites of Chlorine atom in the P-Cresol Methylhydroxylase: Alteration of the Structure of the Flavoprotein Subunit Upon Its Binding to the Cytochrome Subunit (pdb code 1wvf). This binding sites where shown within 5.0 Angstroms radius around Chlorine atom.
In total only one binding site of Chlorine was determined in the P-Cresol Methylhydroxylase: Alteration of the Structure of the Flavoprotein Subunit Upon Its Binding to the Cytochrome Subunit, PDB code: 1wvf:

Chlorine binding site 1 out of 1 in 1wvf

Go back to Chlorine Binding Sites List in 1wvf
Chlorine binding site 1 out of 1 in the P-Cresol Methylhydroxylase: Alteration of the Structure of the Flavoprotein Subunit Upon Its Binding to the Cytochrome Subunit


Mono view


Stereo pair view

A full contact list of Chlorine with other atoms in the Cl binding site number 1 of P-Cresol Methylhydroxylase: Alteration of the Structure of the Flavoprotein Subunit Upon Its Binding to the Cytochrome Subunit within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Cl1703

b:10.5
occ:1.00
 OG A:SER97 3.1 9.4 1.0
N A:GLY96 3.2 7.7 1.0
O A:HOH1797 3.2 13.6 1.0
N A:MET48 3.3 11.0 1.0
N A:GLY94 3.3 7.9 1.0
N A:SER97 3.5 7.8 1.0
CA A:GLY96 3.5 8.0 1.0
C A:GLY96 3.6 7.2 1.0
CB A:MET48 3.6 11.5 1.0
CG A:MET48 3.8 14.6 1.0
SD A:MET49 3.9 12.0 0.5
CA A:MET48 3.9 11.0 1.0
N A:TYR95 3.9 7.2 1.0
CA A:GLY94 3.9 8.1 1.0
CB A:SER97 4.0 7.4 1.0
C A:GLY94 4.2 7.2 1.0
CG A:MET49 4.2 6.8 0.5
C A:ILE47 4.2 11.5 1.0
CA A:ILE47 4.3 10.7 1.0
C A:PHE93 4.3 7.2 1.0
CA A:SER97 4.3 7.8 1.0
O A:ASN92 4.3 7.2 1.0
CA A:PHE93 4.4 7.9 1.0
N A:MET49 4.4 10.4 0.5
C A:TYR95 4.4 8.0 1.0
O A:GLY96 4.4 7.5 1.0
C A:MET48 4.4 10.7 1.0
N A:MET49 4.4 9.7 0.5
SD A:MET48 4.5 15.9 1.0
O A:SER392 4.6 10.9 1.0
CB A:ILE47 4.7 10.2 1.0
CA A:TYR95 4.8 7.7 1.0
CG A:MET49 4.9 11.8 0.5
SD A:MET49 5.0 5.1 0.5
O A:HOH1965 5.0 22.8 1.0

Reference:

L.M.Cunane, Z.-W.Chen, W.S.Mcintire, F.S.Mathews. P-Cresol Methylhydroxylase: Alteration of the Structure of the Flavoprotein Subunit Upon Its Binding to the Cytochrome Subunit Biochemistry V. 44 2963 2005.
ISSN: ISSN 0006-2960
PubMed: 15723539
DOI: 10.1021/BI048020R
Page generated: Thu Jul 10 20:20:46 2025

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