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Potassium in PDB 1nxy: Crystal Structure of the Complex Between M182T Mutant of Tem-1 and A Boronic Acid Inhibitor (SM2)

Enzymatic activity of Crystal Structure of the Complex Between M182T Mutant of Tem-1 and A Boronic Acid Inhibitor (SM2)

All present enzymatic activity of Crystal Structure of the Complex Between M182T Mutant of Tem-1 and A Boronic Acid Inhibitor (SM2):
3.5.2.6;

Protein crystallography data

The structure of Crystal Structure of the Complex Between M182T Mutant of Tem-1 and A Boronic Acid Inhibitor (SM2), PDB code: 1nxy was solved by X.Wang, G.Minasov, J.Blazquez, E.Caselli, 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 / 1.60
Space group P 21 21 21
Cell size a, b, c (Å), α, β, γ (°) 73.625, 34.560, 105.360, 90.00, 90.00, 90.00
R / Rfree (%) 17.2 / 19.6

Potassium Binding Sites:

The binding sites of Potassium atom in the Crystal Structure of the Complex Between M182T Mutant of Tem-1 and A Boronic Acid Inhibitor (SM2) (pdb code 1nxy). 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 Crystal Structure of the Complex Between M182T Mutant of Tem-1 and A Boronic Acid Inhibitor (SM2), PDB code: 1nxy:

Potassium binding site 1 out of 1 in 1nxy

Go back to Potassium Binding Sites List in 1nxy
Potassium binding site 1 out of 1 in the Crystal Structure of the Complex Between M182T Mutant of Tem-1 and A Boronic Acid Inhibitor (SM2)


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 Complex Between M182T Mutant of Tem-1 and A Boronic Acid Inhibitor (SM2) within 5.0Å range:
probe atom residue distance (Å) B Occ
A:K1

b:8.0
occ:0.30
 CB A:ASP214 1.4 9.4 0.7
CG A:ASP214 2.2 8.1 0.7
CA A:ASP214 2.3 9.5 0.7
O A:MET211 2.5 6.6 1.0
O A:ASP233 2.5 6.9 1.0
O A:ALA213 2.6 6.5 0.3
N A:ASP214 2.7 6.4 0.7
OD2 A:ASP214 2.8 9.7 0.7
OD2 A:ASP214 2.9 19.3 0.3
OD1 A:ASP214 3.0 9.5 0.7
OD1 A:ASP233 3.1 7.6 1.0
CG A:ASP214 3.3 16.7 0.3
CB A:ASP214 3.3 14.9 0.3
C A:MET211 3.4 4.9 1.0
C A:ASP233 3.6 7.7 1.0
C A:ALA213 3.6 9.5 0.3
C A:ASP214 3.7 9.2 0.7
CA A:MET211 3.7 8.1 1.0
CA A:ASP214 3.8 12.7 0.3
O A:TRP210 4.0 7.0 1.0
C A:ALA213 4.0 7.0 0.7
N A:ASP233 4.1 4.6 1.0
O A:ILE127 4.1 10.6 1.0
N A:ASP214 4.2 10.7 0.3
NH2 A:ARG222 4.2 8.4 1.0
OD1 A:ASP214 4.3 14.0 0.3
O A:ASP214 4.3 7.9 0.7
CG A:ASP233 4.3 8.9 1.0
CA A:ASP233 4.3 6.9 1.0
CG2 A:ILE127 4.3 5.7 1.0
N A:LYS234 4.5 7.5 1.0
N A:ALA213 4.5 8.3 0.3
N A:LYS215 4.5 11.1 0.7
N A:GLU212 4.6 5.7 1.0
N A:ALA213 4.6 6.7 0.7
CB A:MET211 4.6 7.0 1.0
CA A:LYS234 4.7 7.9 1.0
C A:GLU212 4.7 8.2 1.0
CA A:THR128 4.7 9.9 1.0
N A:MET211 4.8 7.6 1.0
CA A:ALA213 4.8 8.3 0.3
C A:ILE127 4.8 9.3 1.0
O A:ALA213 4.8 6.6 0.7
C A:TRP210 4.8 7.3 1.0
O A:HOH512 4.9 12.2 1.0
CA A:ALA213 4.9 6.5 0.7
CB A:ASP233 4.9 6.3 1.0

Reference:

X.Wang, G.Minasov, J.Blazquez, E.Caselli, F.Prati, B.K.Shoichet. Recognition and Resistance in Tem Beta-Lactamase Biochemistry V. 42 8434 2003.
ISSN: ISSN 0006-2960
PubMed: 12859188
DOI: 10.1021/BI034242Y
Page generated: Mon Aug 12 05:03:47 2024

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