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Potassium in PDB 2as3: Cytochrome C Peroxidase in Complex with Phenol

Enzymatic activity of Cytochrome C Peroxidase in Complex with Phenol

All present enzymatic activity of Cytochrome C Peroxidase in Complex with Phenol:
1.11.1.5;

Protein crystallography data

The structure of Cytochrome C Peroxidase in Complex with Phenol, PDB code: 2as3 was solved by R.Brenk, S.W.Vetter, S.E.Boyce, D.B.Goodin, B.K.Shoichet, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 10.00 / 1.40
Space group P 21 21 21
Cell size a, b, c (Å), α, β, γ (°) 50.980, 75.510, 106.870, 90.00, 90.00, 90.00
R / Rfree (%) n/a / 18.8

Other elements in 2as3:

The structure of Cytochrome C Peroxidase in Complex with Phenol also contains other interesting chemical elements:

Iron (Fe) 1 atom

Potassium Binding Sites:

The binding sites of Potassium atom in the Cytochrome C Peroxidase in Complex with Phenol (pdb code 2as3). 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 Cytochrome C Peroxidase in Complex with Phenol, PDB code: 2as3:

Potassium binding site 1 out of 1 in 2as3

Go back to Potassium Binding Sites List in 2as3
Potassium binding site 1 out of 1 in the Cytochrome C Peroxidase in Complex with Phenol


Mono view


Stereo pair view

A full contact list of Potassium with other atoms in the K binding site number 1 of Cytochrome C Peroxidase in Complex with Phenol within 5.0Å range:
probe atom residue distance (Å) B Occ
A:K600

b:44.6
occ:0.35
C1 A:IPH500 1.4 23.9 0.7
C6 A:IPH500 1.5 20.3 0.7
O1 A:IPH500 1.5 26.2 0.7
O A:LEU177 2.6 17.4 1.0
C2 A:IPH500 2.7 23.0 0.7
C5 A:IPH500 2.7 19.3 0.7
O A:HOH1004 2.8 23.4 0.3
O A:HOH1003 3.0 20.7 0.3
O A:HIS175 3.1 22.2 1.0
O A:HOH1000 3.3 17.7 0.3
C3 A:IPH500 3.6 23.6 0.7
C4 A:IPH500 3.6 22.0 0.7
C A:HIS175 3.7 16.6 1.0
C A:LEU177 3.8 15.3 1.0
CA A:HIS175 3.9 14.5 1.0
N A:LYS179 3.9 16.5 1.0
C A:GLY178 4.0 15.5 1.0
CA A:LYS179 4.1 16.4 1.0
O A:GLY178 4.1 18.4 1.0
CAD A:HEM400 4.1 14.7 1.0
O A:HOH1002 4.2 24.5 0.3
O A:HOH1001 4.3 20.0 0.3
CB A:HIS175 4.3 16.0 1.0
C A:LYS179 4.4 17.9 1.0
C3D A:HEM400 4.4 14.2 1.0
N A:LEU177 4.4 16.5 1.0
CD2 A:HIS175 4.4 14.5 1.0
N A:GLY191 4.5 32.3 1.0
CG A:HIS175 4.5 15.1 1.0
N A:GLY178 4.6 15.1 1.0
CA A:GLY178 4.6 15.9 1.0
C4D A:HEM400 4.7 15.1 1.0
CA A:LEU177 4.7 15.6 1.0
CHA A:HEM400 4.7 16.0 1.0
O A:HOH1557 4.7 42.9 1.0
N A:THR180 4.8 16.6 1.0
O A:LYS179 4.8 18.7 1.0
C A:ALA176 4.8 17.6 1.0
N A:ALA176 4.8 17.2 1.0
O A:ALA174 4.8 15.5 1.0
CA A:GLY191 4.9 36.1 1.0
O A:HOH1000 5.0 21.1 0.7

Reference:

R.Brenk, S.W.Vetter, S.E.Boyce, D.B.Goodin, B.K.Shoichet. Probing Molecular Docking in A Charged Model Binding Site. J.Mol.Biol. V. 357 1449 2006.
ISSN: ISSN 0022-2836
PubMed: 16490206
DOI: 10.1016/J.JMB.2006.01.034
Page generated: Sun Dec 13 23:08:50 2020

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