Atomistry » Chlorine » PDB 1wvf-1xki » 1wvf
Atomistry »
  Chlorine »
    PDB 1wvf-1xki »
      1wvf »

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: Sat Dec 12 08:54:10 2020

Last articles

Zn in 8WB0
Zn in 8WAX
Zn in 8WAU
Zn in 8WAZ
Zn in 8WAY
Zn in 8WAV
Zn in 8WAW
Zn in 8WAT
Zn in 8W7M
Zn in 8WD3
© Copyright 2008-2020 by atomistry.com
Home   |    Site Map   |    Copyright   |    Contact us   |    Privacy