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Potassium in PDB 1cpg: A Cation Binding Motif Stabilizes the Compound I Radical of Cytochrome C Peroxidase

Enzymatic activity of A Cation Binding Motif Stabilizes the Compound I Radical of Cytochrome C Peroxidase

All present enzymatic activity of A Cation Binding Motif Stabilizes the Compound I Radical of Cytochrome C Peroxidase:
1.11.1.5;

Protein crystallography data

The structure of A Cation Binding Motif Stabilizes the Compound I Radical of Cytochrome C Peroxidase, PDB code: 1cpg was solved by M.A.Miller, G.W.Han, J.Kraut, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 20.00 / 2.20
Space group P 21 21 21
Cell size a, b, c (Å), α, β, γ (°) 105.170, 74.180, 45.220, 90.00, 90.00, 90.00
R / Rfree (%) n/a / n/a

Other elements in 1cpg:

The structure of A Cation Binding Motif Stabilizes the Compound I Radical of Cytochrome C Peroxidase also contains other interesting chemical elements:

Iron (Fe) 1 atom

Potassium Binding Sites:

The binding sites of Potassium atom in the A Cation Binding Motif Stabilizes the Compound I Radical of Cytochrome C Peroxidase (pdb code 1cpg). This binding sites where shown within 5.0 Angstroms radius around Potassium atom.
In total only one binding site of Potassium was determined in the A Cation Binding Motif Stabilizes the Compound I Radical of Cytochrome C Peroxidase, PDB code: 1cpg:

Potassium binding site 1 out of 1 in 1cpg

Go back to Potassium Binding Sites List in 1cpg
Potassium binding site 1 out of 1 in the A Cation Binding Motif Stabilizes the Compound I Radical of Cytochrome C Peroxidase


Mono view


Stereo pair view

A full contact list of Potassium with other atoms in the K binding site number 1 of A Cation Binding Motif Stabilizes the Compound I Radical of Cytochrome C Peroxidase within 5.0Å range:
probe atom residue distance (Å) B Occ
A:K975

b:36.8
occ:1.00
 OE1 A:GLN191 2.5 28.1 1.0
O A:LEU177 2.5 28.7 1.0
O A:HIS175 2.6 17.8 1.0
O A:HOH979 2.6 27.7 1.0
CD A:GLN191 3.4 24.1 1.0
C A:HIS175 3.4 16.0 1.0
C A:LEU177 3.6 24.3 1.0
N A:LYS179 3.7 17.5 1.0
C A:GLY178 3.7 18.1 1.0
O A:GLY178 3.8 16.3 1.0
CA A:HIS175 3.8 15.5 1.0
CA A:LYS179 3.8 19.3 1.0
CAD A:HEM296 3.8 20.7 1.0
CG A:GLN191 3.9 12.9 1.0
O A:HOH477 4.1 21.5 1.0
C3D A:HEM296 4.1 20.8 1.0
CB A:HIS175 4.3 19.9 1.0
N A:LEU177 4.3 22.6 1.0
C A:LYS179 4.3 19.6 1.0
O A:HOH978 4.3 23.0 1.0
CD2 A:HIS175 4.4 25.5 1.0
CA A:GLY178 4.4 15.2 1.0
N A:GLY178 4.4 19.6 1.0
CG A:HIS175 4.4 23.8 1.0
NE2 A:GLN191 4.5 29.9 1.0
C A:ALA176 4.5 20.6 1.0
CA A:LEU177 4.5 23.2 1.0
N A:ALA176 4.5 14.8 1.0
CB A:GLN191 4.6 16.3 1.0
C4D A:HEM296 4.6 16.5 1.0
O A:LYS179 4.6 19.0 1.0
CHA A:HEM296 4.6 12.1 1.0
O A:ALA174 4.7 23.9 1.0
C2D A:HEM296 4.8 21.0 1.0
O A:ALA176 4.8 24.6 1.0
N A:THR180 5.0 13.6 1.0
CA A:ALA176 5.0 15.0 1.0

Reference:

M.A.Miller, G.W.Han, J.Kraut. A Cation Binding Motif Stabilizes the Compound I Radical of Cytochrome C Peroxidase. Proc.Natl.Acad.Sci.Usa V. 91 11118 1994.
ISSN: ISSN 0027-8424
PubMed: 7972020
DOI: 10.1073/PNAS.91.23.11118
Page generated: Sat Aug 9 01:44:38 2025

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