Potassium in PDB 3zcg: Ascorbate Peroxidase W41A-H42C Mutant

All present enzymatic activity of Ascorbate Peroxidase W41A-H42C Mutant:
1.11.1.11;

The structure of Ascorbate Peroxidase W41A-H42C Mutant, PDB code: 3zcg 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)	36.10 / 1.49
Space group	P 42 21 2
Cell size a, b, c (Å), α, β, γ (°)	82.270, 82.270, 75.310, 90.00, 90.00, 90.00
R / Rfree (%)	13.8 / 17.2

The structure of Ascorbate Peroxidase W41A-H42C Mutant also contains other interesting chemical elements:

Iron

(Fe)

1 atom

The binding sites of Potassium atom in the Ascorbate Peroxidase W41A-H42C Mutant (pdb code 3zcg). 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 Ascorbate Peroxidase W41A-H42C Mutant, PDB code: 3zcg:

Potassium binding site 1 out of 1 in the Ascorbate Peroxidase W41A-H42C Mutant


Mono view


Stereo pair view

A full contact list of Potassium with other atoms in the K binding site number 1 of Ascorbate Peroxidase W41A-H42C Mutant within 5.0Å range: probe atom residue distance (Å) B Occ A:K1251 b:11.6 occ:1.00 O A:THR164 2.6 7.4 1.0 O A:ILE185 2.6 8.8 1.0 OD1 A:ASN182 2.8 14.8 1.0 O A:ASN182 2.8 8.4 1.0 OG1 A:THR180 2.9 9.1 1.0 OD1 A:ASP187 3.0 10.8 1.0 OG1 A:THR164 3.0 11.0 1.0 OG A:SER189 3.2 12.5 0.4 CG A:ASN182 3.4 12.2 1.0 CB A:THR180 3.5 9.8 1.0 C A:THR164 3.6 5.1 1.0 C A:ASN182 3.7 7.0 1.0 CG2 A:THR180 3.7 9.3 1.0 C A:ILE185 3.8 7.4 1.0 CG A:ASP187 3.9 11.5 1.0 ND2 A:ASN182 3.9 14.8 1.0 CB A:THR164 4.0 7.1 1.0 CA A:THR164 4.2 6.2 1.0 OD2 A:ASP187 4.3 18.5 1.0 CB A:SER189 4.3 11.3 0.6 CB A:ASN182 4.3 12.4 1.0 CA A:ASN182 4.4 10.8 1.0 N A:ASP187 4.4 7.3 1.0 CG2 A:THR164 4.5 7.3 1.0 N A:PRO183 4.5 8.0 1.0 CB A:ILE185 4.5 6.8 1.0 CA A:ILE185 4.5 6.7 1.0 N A:ILE185 4.5 6.2 1.0 CB A:SER189 4.6 13.0 0.4 CA A:PRO183 4.6 8.7 1.0 N A:ASN182 4.6 9.8 1.0 N A:ILE165 4.7 6.1 1.0 OG A:SER189 4.7 16.8 0.6 N A:PHE186 4.9 5.8 1.0 CB A:ASP187 5.0 10.0 1.0

A.Guimero, S.K.Badyal, T.Leeks, P.C.E.Moody, E.L.Raven. Probing the Conformational Mobility of the Active Site of A Heme Peroxidase. Dalton Trans V. 42 3170 2013.
ISSN: ISSN 1477-9226
PubMed: 23202589
DOI: 10.1039/C2DT32455E