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Potassium in PDB 2ffy: Ampc Beta-Lactamase N289A Mutant in Complex with A Boronic Acid Deacylation Transition State Analog Compound SM3

Enzymatic activity of Ampc Beta-Lactamase N289A Mutant in Complex with A Boronic Acid Deacylation Transition State Analog Compound SM3

All present enzymatic activity of Ampc Beta-Lactamase N289A Mutant in Complex with A Boronic Acid Deacylation Transition State Analog Compound SM3:
3.5.2.6;

Protein crystallography data

The structure of Ampc Beta-Lactamase N289A Mutant in Complex with A Boronic Acid Deacylation Transition State Analog Compound SM3, PDB code: 2ffy was solved by Y.Chen, G.Minasov, T.A.Roth, F.Prati, B.K.Shoichet, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 15.00 / 1.07
Space group C 1 2 1
Cell size a, b, c (Å), α, β, γ (°) 118.840, 76.063, 97.898, 90.00, 115.85, 90.00
R / Rfree (%) 13.3 / 16.4

Potassium Binding Sites:

The binding sites of Potassium atom in the Ampc Beta-Lactamase N289A Mutant in Complex with A Boronic Acid Deacylation Transition State Analog Compound SM3 (pdb code 2ffy). This binding sites where shown within 5.0 Angstroms radius around Potassium atom.
In total 2 binding sites of Potassium where determined in the Ampc Beta-Lactamase N289A Mutant in Complex with A Boronic Acid Deacylation Transition State Analog Compound SM3, PDB code: 2ffy:
Jump to Potassium binding site number: 1; 2;

Potassium binding site 1 out of 2 in 2ffy

Go back to Potassium Binding Sites List in 2ffy
Potassium binding site 1 out of 2 in the Ampc Beta-Lactamase N289A Mutant in Complex with A Boronic Acid Deacylation Transition State Analog Compound SM3


Mono view


Stereo pair view

A full contact list of Potassium with other atoms in the K binding site number 1 of Ampc Beta-Lactamase N289A Mutant in Complex with A Boronic Acid Deacylation Transition State Analog Compound SM3 within 5.0Å range:
probe atom residue distance (Å) B Occ
A:K2

b:18.6
occ:0.36
O A:HOH5860 2.5 45.2 1.0
O A:HOH5425 2.6 26.4 1.0
OD1 A:ASP217 2.7 13.1 1.0
O A:HOH5829 2.9 39.9 1.0
O A:GLY214 3.0 14.0 1.0
O A:HOH5862 3.1 51.0 1.0
O A:HOH5553 3.1 23.9 1.0
H A:ASP217 3.4 13.7 1.0
H A:LEU216 3.4 15.4 1.0
HA A:ALA215 3.5 16.9 1.0
CG A:ASP217 3.6 12.2 1.0
O A:HOH5910 3.8 40.0 1.0
N A:LEU216 3.9 12.9 1.0
O A:HOH5909 4.0 38.6 0.5
C A:GLY214 4.0 13.8 1.0
OD2 A:ASP217 4.0 14.4 1.0
H A:ALA218 4.1 14.0 1.0
N A:ASP217 4.2 11.4 1.0
CA A:ALA215 4.2 14.1 1.0
O A:HOH5505 4.3 24.8 1.0
H A:GLY214 4.4 17.7 1.0
C A:ALA215 4.4 12.8 1.0
N A:ALA215 4.6 13.8 1.0
HA A:LEU216 4.6 14.2 1.0
CB A:ASP217 4.7 12.1 1.0
CA A:LEU216 4.7 11.8 1.0
O A:HOH5714 4.8 32.7 1.0
O A:HOH5756 4.8 32.8 1.0
HB3 A:ASP217 4.9 14.5 1.0
C A:LEU216 5.0 10.9 1.0
N A:GLY214 5.0 14.7 1.0
CA A:ASP217 5.0 11.1 1.0
N A:ALA218 5.0 11.7 1.0

Potassium binding site 2 out of 2 in 2ffy

Go back to Potassium Binding Sites List in 2ffy
Potassium binding site 2 out of 2 in the Ampc Beta-Lactamase N289A Mutant in Complex with A Boronic Acid Deacylation Transition State Analog Compound SM3


Mono view


Stereo pair view

A full contact list of Potassium with other atoms in the K binding site number 2 of Ampc Beta-Lactamase N289A Mutant in Complex with A Boronic Acid Deacylation Transition State Analog Compound SM3 within 5.0Å range:
probe atom residue distance (Å) B Occ
B:K3

b:11.0
occ:0.36
O B:HOH9407 2.7 19.0 1.0
O B:GLY214 2.8 12.5 1.0
O B:HOH9478 2.8 10.5 0.5
OD1 B:ASP217 2.9 12.1 1.0
O B:HOH9548 2.9 25.6 1.0
O B:HOH9546 2.9 29.1 1.0
H B:LEU216 3.2 13.7 1.0
HA B:ALA215 3.2 15.5 1.0
H B:ASP217 3.3 12.7 1.0
CG B:ASP217 3.7 11.6 1.0
N B:LEU216 3.7 11.4 1.0
C B:GLY214 3.8 12.1 1.0
CA B:ALA215 4.0 12.9 1.0
N B:ASP217 4.1 10.6 1.0
O B:HOH9634 4.1 17.6 0.5
OD2 B:ASP217 4.1 12.9 1.0
C B:ALA215 4.2 11.3 1.0
H B:ALA218 4.2 12.8 1.0
N B:ALA215 4.3 12.7 1.0
H B:GLY214 4.3 16.3 1.0
HA B:LEU216 4.4 13.6 1.0
CA B:LEU216 4.6 11.3 1.0
O B:HOH9617 4.6 30.4 1.0
O B:HOH9591 4.7 34.3 1.0
CB B:ASP217 4.7 11.0 1.0
C B:LEU216 4.8 9.8 1.0
O B:HOH9527 4.9 15.3 0.5
HB3 B:ASP217 4.9 13.2 1.0
N B:GLY214 4.9 13.6 1.0
CA B:ASP217 4.9 10.2 1.0
CA B:GLY214 5.0 14.0 1.0

Reference:

Y.Chen, G.Minasov, T.A.Roth, F.Prati, B.K.Shoichet. The Deacylation Mechanism of Ampc Beta-Lactamase at Ultrahigh Resolution J.Am.Chem.Soc. V. 128 2970 2006.
ISSN: ISSN 0002-7863
PubMed: 16506777
DOI: 10.1021/JA056806M
Page generated: Sun Dec 13 23:09:46 2020

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