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Potassium in PDB 1krj: Engineering Calcium-Binding Site Into Cytochrome C Peroxidase (Ccp)

Enzymatic activity of Engineering Calcium-Binding Site Into Cytochrome C Peroxidase (Ccp)

All present enzymatic activity of Engineering Calcium-Binding Site Into Cytochrome C Peroxidase (Ccp):
1.11.1.5;

Protein crystallography data

The structure of Engineering Calcium-Binding Site Into Cytochrome C Peroxidase (Ccp), PDB code: 1krj was solved by C.A.Bonagura, B.Bhaskar, M.Sundaramoorthy, T.L.Poulos, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 10.00 / 2.00
Space group P 21 21 21
Cell size a, b, c (Å), α, β, γ (°) 107.034, 75.458, 51.100, 90.00, 90.00, 90.00
R / Rfree (%) 19.2 / n/a

Other elements in 1krj:

The structure of Engineering Calcium-Binding Site Into Cytochrome C Peroxidase (Ccp) also contains other interesting chemical elements:

Iron (Fe) 1 atom

Potassium Binding Sites:

The binding sites of Potassium atom in the Engineering Calcium-Binding Site Into Cytochrome C Peroxidase (Ccp) (pdb code 1krj). 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 Engineering Calcium-Binding Site Into Cytochrome C Peroxidase (Ccp), PDB code: 1krj:

Potassium binding site 1 out of 1 in 1krj

Go back to Potassium Binding Sites List in 1krj
Potassium binding site 1 out of 1 in the Engineering Calcium-Binding Site Into Cytochrome C Peroxidase (Ccp)


Mono view


Stereo pair view

A full contact list of Potassium with other atoms in the K binding site number 1 of Engineering Calcium-Binding Site Into Cytochrome C Peroxidase (Ccp) within 5.0Å range:
probe atom residue distance (Å) B Occ
A:K500

b:14.4
occ:1.00
 O A:THR194 2.1 15.2 1.0
OG1 A:THR176 2.3 17.6 1.0
O A:THR176 2.4 14.2 1.0
OG1 A:THR194 2.4 20.8 1.0
O A:VAL197 2.5 14.6 1.0
OD2 A:ASP192 2.5 21.3 1.0
OD1 A:ASP199 2.6 14.2 1.0
OD1 A:ASP192 3.1 14.2 1.0
C A:THR194 3.1 16.2 1.0
CG A:ASP192 3.2 17.0 1.0
C A:THR176 3.4 12.7 1.0
CB A:THR194 3.5 15.8 1.0
CG A:ASP199 3.5 14.3 1.0
CB A:THR176 3.5 13.2 1.0
C A:VAL197 3.7 13.8 1.0
CA A:THR176 3.8 14.1 1.0
CA A:THR194 3.8 17.3 1.0
OD2 A:ASP199 3.8 16.7 1.0
N A:THR194 4.2 17.3 1.0
N A:ASN195 4.2 15.1 1.0
N A:ASP199 4.2 13.9 1.0
CG2 A:THR176 4.2 12.0 1.0
N A:VAL197 4.4 10.5 1.0
CA A:ASN195 4.4 19.8 1.0
CA A:VAL197 4.5 11.7 1.0
N A:LEU177 4.6 12.5 1.0
CB A:ASP192 4.6 14.5 1.0
CB A:VAL197 4.6 9.8 1.0
N A:PHE198 4.7 10.7 1.0
O A:HOH440 4.7 21.8 1.0
CA A:PHE198 4.8 11.3 1.0
O A:ASP199 4.8 15.7 1.0
CB A:ASP199 4.8 13.9 1.0
CG2 A:THR194 4.8 15.7 1.0
C A:ASN195 4.9 18.7 1.0
C A:PHE198 4.9 13.3 1.0
CB A:SER201 4.9 13.0 1.0
CA A:ASP199 4.9 12.9 1.0

Reference:

C.A.Bonagura, B.Bhaskar, M.Sundaramoorthy, T.L.Poulos. Conversion of An Engineered Potassium-Binding Site Into A Calcium-Selective Site in Cytochrome C Peroxidase. J.Biol.Chem. V. 274 37827 1999.
ISSN: ISSN 0021-9258
PubMed: 10608846
DOI: 10.1074/JBC.274.53.37827
Page generated: Mon Aug 12 04:48:08 2024

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