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Potassium in PDB 1stq: Cyrstal Structure of Cytochrome C Peroxidase Mutant: CCPK2M3

Enzymatic activity of Cyrstal Structure of Cytochrome C Peroxidase Mutant: CCPK2M3

All present enzymatic activity of Cyrstal Structure of Cytochrome C Peroxidase Mutant: CCPK2M3:
1.11.1.5;

Protein crystallography data

The structure of Cyrstal Structure of Cytochrome C Peroxidase Mutant: CCPK2M3, PDB code: 1stq was solved by T.P.Barrows, B.Bhaskar, T.L.Poulos, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 50.00 / 1.82
Space group P 21 21 21
Cell size a, b, c (Å), α, β, γ (°) 106.788, 75.692, 51.281, 90.00, 90.00, 90.00
R / Rfree (%) 19.2 / 21.6

Other elements in 1stq:

The structure of Cyrstal Structure of Cytochrome C Peroxidase Mutant: CCPK2M3 also contains other interesting chemical elements:

Iron (Fe) 1 atom

Potassium Binding Sites:

The binding sites of Potassium atom in the Cyrstal Structure of Cytochrome C Peroxidase Mutant: CCPK2M3 (pdb code 1stq). 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 Cyrstal Structure of Cytochrome C Peroxidase Mutant: CCPK2M3, PDB code: 1stq:

Potassium binding site 1 out of 1 in 1stq

Go back to Potassium Binding Sites List in 1stq
Potassium binding site 1 out of 1 in the Cyrstal Structure of Cytochrome C Peroxidase Mutant: CCPK2M3


Mono view


Stereo pair view

A full contact list of Potassium with other atoms in the K binding site number 1 of Cyrstal Structure of Cytochrome C Peroxidase Mutant: CCPK2M3 within 5.0Å range:
probe atom residue distance (Å) B Occ
A:K601

b:3.9
occ:0.70
O A:VAL197 2.6 8.7 1.0
OG1 A:THR176 2.7 12.8 1.0
O A:ASN194 2.7 11.6 1.0
O A:THR176 2.8 10.5 1.0
OD1 A:ASN194 3.0 11.7 1.0
OD1 A:ASP199 3.0 11.1 1.0
OG1 A:THR192 3.2 11.4 1.0
OG A:SER201 3.2 12.4 1.0
CG A:ASN194 3.4 12.2 1.0
C A:ASN194 3.6 11.8 1.0
C A:THR176 3.7 10.6 1.0
ND2 A:ASN194 3.7 12.1 1.0
CG A:ASP199 3.8 11.2 1.0
C A:VAL197 3.8 9.6 1.0
CB A:THR176 3.8 11.9 1.0
CB A:THR192 4.0 10.9 1.0
CA A:THR176 4.1 10.6 1.0
OD2 A:ASP199 4.1 11.9 1.0
CA A:ASN195 4.2 11.6 1.0
N A:ASP199 4.3 9.4 1.0
N A:ASN195 4.3 11.7 1.0
CG2 A:THR192 4.3 10.9 1.0
CB A:ASN194 4.5 11.8 1.0
CA A:ASN194 4.5 12.0 1.0
N A:VAL197 4.5 9.6 1.0
CB A:SER201 4.6 10.7 1.0
CA A:VAL197 4.7 9.7 1.0
N A:LEU177 4.8 9.9 1.0
N A:PHE198 4.8 9.3 1.0
CA A:PHE198 4.8 9.4 1.0
C A:ASN195 4.8 11.3 1.0
CB A:VAL197 4.8 10.2 1.0
CB A:ASP199 4.8 10.4 1.0
N A:ASN194 4.8 11.8 1.0
C A:PHE198 4.9 9.5 1.0
O A:ASP199 5.0 9.3 1.0
CA A:ASP199 5.0 9.7 1.0
CG2 A:THR176 5.0 11.2 1.0

Reference:

T.P.Barrows, B.Bhaskar, T.L.Poulos. Electrostatic Control of the Tryptophan Radical in Cytochrome C Peroxidase. Biochemistry V. 43 8826 2004.
ISSN: ISSN 0006-2960
PubMed: 15236591
DOI: 10.1021/BI049531G
Page generated: Mon Aug 12 05:22:34 2024

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