Potassium in PDB 6mgy: Crystal Structure of the New Deli Metallo Beta Lactamase Variant 5 From Klebsiella Pneumoniae

Protein crystallography data

The structure of Crystal Structure of the New Deli Metallo Beta Lactamase Variant 5 From Klebsiella Pneumoniae, PDB code: 6mgy was solved by Y.Kim, C.Tesar, R.Jedrzejczak, G.Babnigg, A.Joachimiak, Center Forstructural Genomics Of Infectious Diseases (Csgid), with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 30.56 / 1.60
Space group P 1
Cell size a, b, c (Å), α, β, γ (°) 46.869, 69.619, 68.789, 92.26, 103.36, 88.52
R / Rfree (%) 15.4 / 18.9

Other elements in 6mgy:

The structure of Crystal Structure of the New Deli Metallo Beta Lactamase Variant 5 From Klebsiella Pneumoniae also contains other interesting chemical elements:

Zinc (Zn) 8 atoms

Potassium Binding Sites:

The binding sites of Potassium atom in the Crystal Structure of the New Deli Metallo Beta Lactamase Variant 5 From Klebsiella Pneumoniae (pdb code 6mgy). This binding sites where shown within 5.0 Angstroms radius around Potassium atom.
In total 2 binding sites of Potassium where determined in the Crystal Structure of the New Deli Metallo Beta Lactamase Variant 5 From Klebsiella Pneumoniae, PDB code: 6mgy:
Jump to Potassium binding site number: 1; 2;

Potassium binding site 1 out of 2 in 6mgy

Go back to Potassium Binding Sites List in 6mgy
Potassium binding site 1 out of 2 in the Crystal Structure of the New Deli Metallo Beta Lactamase Variant 5 From Klebsiella Pneumoniae


Mono view


Stereo pair view

A full contact list of Potassium with other atoms in the K binding site number 1 of Crystal Structure of the New Deli Metallo Beta Lactamase Variant 5 From Klebsiella Pneumoniae within 5.0Å range:
probe atom residue distance (Å) B Occ
A:K303

b:32.7
occ:1.00
O A:ALA224 2.4 28.5 1.0
O D:ALA224 2.5 29.0 1.0
O A:HOH503 2.8 38.8 1.0
O D:HOH432 2.9 44.4 1.0
O D:GLY222 3.1 27.1 1.0
O A:GLY222 3.2 29.8 1.0
C A:ALA224 3.7 24.4 1.0
C D:ALA224 3.7 25.1 1.0
C D:GLY222 4.0 30.0 1.0
C A:GLY222 4.1 27.8 1.0
O A:HOH412 4.3 35.4 1.0
N A:ALA224 4.4 21.4 1.0
N D:ALA224 4.5 22.6 1.0
CA A:ASP225 4.5 21.4 1.0
N A:ASP225 4.5 21.8 1.0
CA D:ASP225 4.5 21.3 1.0
N D:ASP225 4.5 20.8 1.0
O A:LEU221 4.6 26.2 1.0
N A:THR226 4.6 23.2 1.0
CA A:ALA224 4.6 20.1 1.0
CA D:GLY222 4.7 30.3 1.0
O D:LEU221 4.7 28.8 1.0
N D:THR226 4.7 23.0 1.0
CA D:ALA224 4.7 22.8 1.0
CA A:GLY222 4.8 29.0 1.0
C A:ASP223 4.8 26.5 1.0
C D:ASP223 4.9 23.4 1.0
OG1 A:THR226 4.9 24.2 1.0
OG1 D:THR226 4.9 27.7 1.0
N D:ASP223 4.9 29.7 1.0
N A:ASP223 5.0 25.3 1.0

Potassium binding site 2 out of 2 in 6mgy

Go back to Potassium Binding Sites List in 6mgy
Potassium binding site 2 out of 2 in the Crystal Structure of the New Deli Metallo Beta Lactamase Variant 5 From Klebsiella Pneumoniae


Mono view


Stereo pair view

A full contact list of Potassium with other atoms in the K binding site number 2 of Crystal Structure of the New Deli Metallo Beta Lactamase Variant 5 From Klebsiella Pneumoniae within 5.0Å range:
probe atom residue distance (Å) B Occ
B:K304

b:30.1
occ:1.00
O C:ALA224 2.4 23.1 1.0
O B:ALA224 2.5 24.5 1.0
O B:HOH521 2.8 40.8 1.0
O B:GLY222 3.1 24.6 1.0
O C:GLY222 3.1 26.5 1.0
C C:ALA224 3.6 21.1 1.0
C B:ALA224 3.7 22.4 1.0
C C:GLY222 4.1 25.9 1.0
C B:GLY222 4.1 23.9 1.0
O B:HOH443 4.1 24.6 1.0
N C:ALA224 4.4 20.8 1.0
N B:ALA224 4.4 18.5 1.0
N C:ASP225 4.5 19.9 1.0
CA C:ASP225 4.5 18.8 1.0
CA B:ASP225 4.5 18.3 1.0
N B:ASP225 4.6 18.9 1.0
CA C:ALA224 4.6 19.4 1.0
CA C:GLY222 4.6 31.8 1.0
N C:THR226 4.6 20.9 1.0
CA B:ALA224 4.7 16.9 1.0
N B:THR226 4.7 18.7 1.0
CA B:GLY222 4.7 24.1 1.0
O B:LEU221 4.7 21.0 1.0
C C:ASP223 4.8 22.8 1.0
OG1 B:THR226 4.8 22.8 1.0
O C:LEU221 4.8 28.6 1.0
C B:ASP223 4.8 20.8 1.0
OG1 C:THR226 4.9 22.8 1.0
N C:ASP223 4.9 26.2 1.0
N B:ASP223 5.0 23.6 1.0

Reference:

Y.Kim, C.Tesar, R.Jedrzejczak, G.Babnigg, A.Joachimiak, Center For Structural Genomics Of Infectious Diseases(Csgid). Crystal Structure of the New Deli Metallo Beta Lactamase Variant 5 From Klebsiella Pneumoniae To Be Published.
Page generated: Mon Dec 14 00:53:00 2020

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