Atomistry » Potassium » PDB 2w0f-2xo0 » 2xih
Atomistry »
  Potassium »
    PDB 2w0f-2xo0 »
      2xih »

Potassium in PDB 2xih: The Structure of Ascorbate Peroxidase Compound III

Enzymatic activity of The Structure of Ascorbate Peroxidase Compound III

All present enzymatic activity of The Structure of Ascorbate Peroxidase Compound III:
1.11.1.11;

Protein crystallography data

The structure of The Structure of Ascorbate Peroxidase Compound III, PDB code: 2xih was solved by A.Gumiero, E.L.Raven, P.C.E.Moody, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 35.99 / 1.65
Space group P 42 21 2
Cell size a, b, c (Å), α, β, γ (°) 81.960, 81.960, 75.198, 90.00, 90.00, 90.00
R / Rfree (%) 16.1 / 20.1

Other elements in 2xih:

The structure of The Structure of Ascorbate Peroxidase Compound III also contains other interesting chemical elements:

Iron (Fe) 1 atom

Potassium Binding Sites:

The binding sites of Potassium atom in the The Structure of Ascorbate Peroxidase Compound III (pdb code 2xih). 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 The Structure of Ascorbate Peroxidase Compound III, PDB code: 2xih:

Potassium binding site 1 out of 1 in 2xih

Go back to Potassium Binding Sites List in 2xih
Potassium binding site 1 out of 1 in the The Structure of Ascorbate Peroxidase Compound III


Mono view


Stereo pair view

A full contact list of Potassium with other atoms in the K binding site number 1 of The Structure of Ascorbate Peroxidase Compound III within 5.0Å range:
probe atom residue distance (Å) B Occ
A:K1253

b:14.9
occ:1.00
O A:ILE185 2.6 15.8 1.0
O A:THR164 2.6 11.7 1.0
O A:ASN182 2.7 16.2 1.0
OD1 A:ASN182 2.7 19.0 1.0
OD1 A:ASP187 2.9 14.9 1.0
OG1 A:THR180 3.0 14.3 1.0
OG1 A:THR164 3.1 15.8 1.0
CG A:ASN182 3.3 25.6 1.0
CB A:THR180 3.6 13.2 1.0
C A:ASN182 3.7 14.9 1.0
C A:THR164 3.7 12.0 1.0
CG A:ASP187 3.7 20.9 1.0
C A:ILE185 3.8 18.7 1.0
CG2 A:THR180 3.8 12.7 1.0
ND2 A:ASN182 3.9 19.0 1.0
CB A:SER189 4.1 17.4 1.0
CB A:THR164 4.1 12.0 1.0
OD2 A:ASP187 4.2 19.4 1.0
CA A:THR164 4.2 9.5 1.0
CB A:ASN182 4.3 15.5 1.0
N A:ASP187 4.4 12.9 1.0
CA A:ASN182 4.4 12.5 1.0
N A:PRO183 4.5 12.8 1.0
CB A:ILE185 4.5 13.4 1.0
CA A:ILE185 4.5 14.5 1.0
CG2 A:THR164 4.5 10.4 1.0
CA A:PRO183 4.5 11.4 1.0
N A:ILE185 4.5 11.8 1.0
N A:ASN182 4.6 15.7 1.0
OG A:SER189 4.6 24.2 1.0
N A:ILE165 4.8 14.1 1.0
CB A:ASP187 4.8 14.6 1.0
N A:PHE186 4.8 12.0 1.0
O A:ASP187 4.9 13.7 1.0
CG2 A:ILE185 4.9 15.5 1.0
CA A:PHE186 5.0 12.3 1.0
CG2 A:ILE165 5.0 13.2 1.0

Reference:

A.Gumiero, C.L.Metcalfe, A.R.Pearson, E.L.Raven, P.C.Moody. Nature of the Ferryl Heme in Compounds I and II. J. Biol. Chem. V. 286 1260 2011.
ISSN: ESSN 1083-351X
PubMed: 21062738
DOI: 10.1074/JBC.M110.183483
Page generated: Sun Dec 13 23:13:41 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