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Potassium in PDB 7s10: Crystal Structure of Ascorbate Peroxidase Triple Mutant: S160M, L203M, Q204M

Enzymatic activity of Crystal Structure of Ascorbate Peroxidase Triple Mutant: S160M, L203M, Q204M

All present enzymatic activity of Crystal Structure of Ascorbate Peroxidase Triple Mutant: S160M, L203M, Q204M:
1.11.1.11;

Protein crystallography data

The structure of Crystal Structure of Ascorbate Peroxidase Triple Mutant: S160M, L203M, Q204M, PDB code: 7s10 was solved by T.L.Poulos, J.Kim, V.Murarka, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 36.23 / 1.40
Space group P 42 21 2
Cell size a, b, c (Å), α, β, γ (°) 82.644, 82.644, 75.322, 90, 90, 90
R / Rfree (%) 17.1 / 20.8

Other elements in 7s10:

The structure of Crystal Structure of Ascorbate Peroxidase Triple Mutant: S160M, L203M, Q204M also contains other interesting chemical elements:

Iron (Fe) 1 atom

Potassium Binding Sites:

The binding sites of Potassium atom in the Crystal Structure of Ascorbate Peroxidase Triple Mutant: S160M, L203M, Q204M (pdb code 7s10). 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 Crystal Structure of Ascorbate Peroxidase Triple Mutant: S160M, L203M, Q204M, PDB code: 7s10:

Potassium binding site 1 out of 1 in 7s10

Go back to Potassium Binding Sites List in 7s10
Potassium binding site 1 out of 1 in the Crystal Structure of Ascorbate Peroxidase Triple Mutant: S160M, L203M, Q204M


Mono view


Stereo pair view

A full contact list of Potassium with other atoms in the K binding site number 1 of Crystal Structure of Ascorbate Peroxidase Triple Mutant: S160M, L203M, Q204M within 5.0Å range:
probe atom residue distance (Å) B Occ
A:K304

b:18.8
occ:1.00
 O A:ILE185 2.5 17.8 1.0
O A:THR164 2.6 17.3 1.0
O A:ASN182 2.7 17.6 1.0
OD1 A:ASN182 2.8 22.2 1.0
OG1 A:THR164 3.2 26.6 1.0
OG1 A:THR180 3.3 21.1 1.0
CG A:ASN182 3.4 27.3 1.0
OD1 A:ASP187 3.4 25.3 1.0
C A:THR164 3.6 17.6 1.0
C A:ASN182 3.7 19.0 1.0
C A:ILE185 3.7 17.7 1.0
OG A:SER189 3.8 36.3 0.5
ND2 A:ASN182 3.8 26.3 1.0
CB A:THR180 3.9 19.1 1.0
CG A:ASP187 4.0 27.5 1.0
CG2 A:THR180 4.1 21.4 1.0
CA A:THR164 4.1 17.0 1.0
CB A:THR164 4.2 18.3 1.0
OD2 A:ASP187 4.3 32.8 1.0
CB A:ASN182 4.3 23.9 1.0
CB A:SER189 4.4 14.3 0.5
CA A:ASN182 4.4 20.5 1.0
N A:ILE185 4.4 16.9 1.0
CA A:ILE185 4.4 17.4 1.0
N A:ASP187 4.4 17.9 1.0
CB A:ILE185 4.4 17.3 1.0
N A:PRO183 4.5 18.9 1.0
CA A:PRO183 4.5 19.7 1.0
N A:ASN182 4.6 20.5 1.0
CG2 A:THR164 4.6 18.0 1.0
N A:ILE165 4.7 17.9 1.0
CB A:SER189 4.7 38.9 0.5
OG A:SER189 4.8 21.3 0.5
N A:PHE186 4.8 15.5 1.0
CA A:PHE186 5.0 14.8 1.0
CG2 A:ILE165 5.0 17.7 1.0

Reference:

T.L.Poulos, J.S.Kim, V.C.Murarka. Computational Analysis of the Tryptophan Cation Radical Energetics in Peroxidase Compound I. J.Biol.Inorg.Chem. V. 27 229 2022.
ISSN: ESSN 1432-1327
PubMed: 35064363
DOI: 10.1007/S00775-022-01925-8
Page generated: Wed Apr 5 10:17:51 2023

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