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Potassium in PDB 5jqr: The Structure of Ascorbate Peroxidase Compound II Formed By Reaction with M-Cpba

Enzymatic activity of The Structure of Ascorbate Peroxidase Compound II Formed By Reaction with M-Cpba

All present enzymatic activity of The Structure of Ascorbate Peroxidase Compound II Formed By Reaction with M-Cpba:
1.11.1.11;

Protein crystallography data

The structure of The Structure of Ascorbate Peroxidase Compound II Formed By Reaction with M-Cpba, PDB code: 5jqr was solved by H.Kwon, 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) 58.00 / 1.81
Space group P 42 21 2
Cell size a, b, c (Å), α, β, γ (°) 82.095, 82.095, 75.162, 90.00, 90.00, 90.00
R / Rfree (%) 15.4 / 21.4

Other elements in 5jqr:

The structure of The Structure of Ascorbate Peroxidase Compound II Formed By Reaction with M-Cpba 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 II Formed By Reaction with M-Cpba (pdb code 5jqr). 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 II Formed By Reaction with M-Cpba, PDB code: 5jqr:

Potassium binding site 1 out of 1 in 5jqr

Go back to Potassium Binding Sites List in 5jqr
Potassium binding site 1 out of 1 in the The Structure of Ascorbate Peroxidase Compound II Formed By Reaction with M-Cpba


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 II Formed By Reaction with M-Cpba within 5.0Å range:
probe atom residue distance (Å) B Occ
A:K302

b:15.1
occ:1.00
 O A:ILE185 2.6 8.7 1.0
O A:THR164 2.7 9.7 1.0
OD1 A:ASN182 2.7 14.2 1.0
O A:ASN182 2.8 13.4 1.0
OG1 A:THR180 2.9 9.2 1.0
OD1 A:ASP187 3.0 12.6 1.0
OG1 A:THR164 3.0 10.3 1.0
CG A:ASN182 3.4 17.6 1.0
CB A:THR180 3.6 10.1 1.0
C A:THR164 3.7 8.8 1.0
C A:ASN182 3.7 12.1 1.0
C A:ILE185 3.8 9.6 1.0
CG A:ASP187 3.8 14.1 1.0
CG2 A:THR180 3.8 10.5 1.0
ND2 A:ASN182 3.9 19.7 1.0
CB A:THR164 4.0 9.6 1.0
CA A:THR164 4.1 8.5 1.0
CB A:SER189 4.2 14.6 1.0
OD2 A:ASP187 4.2 16.6 1.0
N A:ASP187 4.4 10.4 1.0
CB A:ASN182 4.4 15.1 1.0
CA A:ASN182 4.4 14.1 1.0
N A:PRO183 4.5 12.1 1.0
CG2 A:THR164 4.5 9.0 1.0
N A:ILE185 4.5 10.2 1.0
CA A:ILE185 4.5 10.1 1.0
CB A:ILE185 4.5 10.9 1.0
CA A:PRO183 4.6 12.3 1.0
OG A:SER189 4.6 19.6 1.0
N A:ASN182 4.6 12.8 1.0
N A:ILE165 4.7 9.7 1.0
N A:PHE186 4.8 9.0 1.0
CB A:ASP187 4.9 12.5 1.0
O A:ASP187 4.9 11.3 1.0
CG2 A:ILE165 5.0 8.9 1.0
CA A:PHE186 5.0 8.0 1.0

Reference:

H.Kwon, J.Basran, C.M.Casadei, A.J.Fielding, T.E.Schrader, A.Ostermann, J.M.Devos, P.Aller, M.P.Blakeley, P.C.Moody, E.L.Raven. Direct Visualization of A Fe(IV)-Oh Intermediate in A Heme Enzyme. Nat Commun V. 7 13445 2016.
ISSN: ESSN 2041-1723
PubMed: 27897163
DOI: 10.1038/NCOMMS13445
Page generated: Sat Aug 9 09:19:14 2025

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