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Potassium in PDB 3fkw: Ampc K67R Mutant Apo Structure

Enzymatic activity of Ampc K67R Mutant Apo Structure

All present enzymatic activity of Ampc K67R Mutant Apo Structure:
3.5.2.6;

Protein crystallography data

The structure of Ampc K67R Mutant Apo Structure, PDB code: 3fkw was solved by Y.Chen, A.Mcreynolds, B.K.Shoichet, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 88.05 / 1.50
Space group C 1 2 1
Cell size a, b, c (Å), α, β, γ (°) 118.348, 76.564, 97.702, 90.00, 115.82, 90.00
R / Rfree (%) 16.6 / 19.9

Potassium Binding Sites:

The binding sites of Potassium atom in the Ampc K67R Mutant Apo Structure (pdb code 3fkw). 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 Ampc K67R Mutant Apo Structure, PDB code: 3fkw:

Potassium binding site 1 out of 1 in 3fkw

Go back to Potassium Binding Sites List in 3fkw
Potassium binding site 1 out of 1 in the Ampc K67R Mutant Apo Structure


Mono view


Stereo pair view

A full contact list of Potassium with other atoms in the K binding site number 1 of Ampc K67R Mutant Apo Structure within 5.0Å range:
probe atom residue distance (Å) B Occ
B:K504

b:20.3
occ:1.00
O B:HOH1420 2.9 19.2 1.0
O A:HOH1232 3.1 18.6 1.0
O B:HOH1166 3.3 22.7 1.0
O A:HOH1149 3.3 28.1 1.0
CA A:PRO303 3.7 13.8 1.0
CA B:PRO303 3.8 13.6 1.0
CD A:PRO304 3.8 15.1 1.0
CG2 B:THR302 3.8 16.4 1.0
CA B:THR302 3.9 14.6 1.0
CG2 A:THR302 4.1 14.4 1.0
CD B:PRO304 4.1 13.4 1.0
CA A:THR302 4.1 13.2 1.0
CB A:PRO303 4.3 14.1 1.0
CB B:THR302 4.3 15.2 1.0
O B:ILE301 4.3 13.9 1.0
O A:ILE301 4.4 14.2 1.0
CB B:PRO303 4.4 14.2 1.0
OG1 B:THR302 4.4 16.2 1.0
N B:PRO303 4.4 13.9 1.0
N A:PRO303 4.5 13.6 1.0
CB A:THR302 4.5 13.7 1.0
C B:THR302 4.6 14.1 1.0
N A:PRO304 4.6 14.3 1.0
OG1 A:THR302 4.6 15.1 1.0
C A:PRO303 4.6 14.0 1.0
O B:HOH1664 4.7 20.2 1.0
C A:THR302 4.7 13.3 1.0
C B:PRO303 4.7 13.4 1.0
N B:PRO304 4.7 13.0 1.0
CG A:PRO304 4.8 15.2 1.0
O B:HOH1672 4.9 17.6 1.0
O A:HOH1667 4.9 18.4 1.0
CG B:PRO304 4.9 13.6 1.0
N B:THR302 5.0 13.9 1.0

Reference:

Y.Chen, A.Mcreynolds, B.K.Shoichet. Re-Examining the Role of LYS67 in Class C Beta-Lactamase Catalysis. Protein Sci. V. 18 662 2009.
ISSN: ISSN 0961-8368
PubMed: 19241376
DOI: 10.1002/PRO.60
Page generated: Mon Aug 12 08:20:06 2024

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