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Potassium in PDB 8dod: Beta-Lactamase Ctx-M-14 S130A

Enzymatic activity of Beta-Lactamase Ctx-M-14 S130A

All present enzymatic activity of Beta-Lactamase Ctx-M-14 S130A:
3.5.2.6;

Protein crystallography data

The structure of Beta-Lactamase Ctx-M-14 S130A, PDB code: 8dod was solved by S.Lu, T.Palzkill, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 35.50 / 1.61
Space group P 32 2 1
Cell size a, b, c (Å), α, β, γ (°) 41.49, 41.49, 230.78, 90, 90, 120
R / Rfree (%) 22.2 / 25.9

Potassium Binding Sites:

The binding sites of Potassium atom in the Beta-Lactamase Ctx-M-14 S130A (pdb code 8dod). 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 Beta-Lactamase Ctx-M-14 S130A, PDB code: 8dod:

Potassium binding site 1 out of 1 in 8dod

Go back to Potassium Binding Sites List in 8dod
Potassium binding site 1 out of 1 in the Beta-Lactamase Ctx-M-14 S130A


Mono view


Stereo pair view

A full contact list of Potassium with other atoms in the K binding site number 1 of Beta-Lactamase Ctx-M-14 S130A within 5.0Å range:
probe atom residue distance (Å) B Occ
A:K301

b:15.8
occ:1.00
O A:ALA130 2.7 18.9 1.0
O A:HOH536 2.8 31.2 1.0
O A:HOH543 3.0 36.4 1.0
OD1 A:ASN132 3.0 21.1 1.0
CB A:ALA130 3.2 38.6 1.0
O A:HOH482 3.3 24.1 1.0
HD2 A:TYR105 3.3 21.1 1.0
HZ2 A:LYS73 3.5 32.1 1.0
HB2 A:SER70 3.5 21.5 1.0
HD21 A:ASN132 3.5 32.3 1.0
O A:HOH540 3.6 42.0 1.0
C A:ALA130 3.6 30.8 1.0
CG A:ASN132 3.8 33.8 1.0
HZ1 A:LYS73 3.8 32.1 1.0
OG A:SER70 3.8 24.8 1.0
CA A:ALA130 3.9 36.5 1.0
ND2 A:ASN132 4.0 26.9 1.0
O A:HOH420 4.0 24.4 1.0
NZ A:LYS73 4.0 26.7 1.0
CD2 A:TYR105 4.1 17.6 1.0
HE2 A:LYS73 4.1 45.8 1.0
HA A:ALA130 4.1 43.9 1.0
CB A:SER70 4.2 17.9 1.0
HB3 A:TYR105 4.3 22.4 1.0
HE2 A:TYR105 4.4 21.3 1.0
HB3 A:SER70 4.6 21.5 1.0
CE A:LYS73 4.6 38.1 1.0
CE2 A:TYR105 4.7 17.8 1.0
HD22 A:ASN132 4.8 32.3 1.0
HZ3 A:LYS73 4.8 32.1 1.0
HZ1 A:LYS234 4.8 24.7 1.0
N A:ASP131 4.9 15.6 1.0
H A:ASN132 4.9 21.3 1.0
CG A:TYR105 4.9 23.6 1.0
O A:HOH492 5.0 33.5 1.0

Reference:

S.Lu, M.Montoya, L.Hu, N.Neetu, B.Sankaran, B.V.V.Prasad, T.Palzkill. Mutagenesis and Structural Analysis Reveal the Ctx-M Beta-Lactamase Active Site Is Optimized For Cephalosporin Catalysis and Drug Resistance. J.Biol.Chem. 04630 2023.
ISSN: ESSN 1083-351X
PubMed: 36963495
DOI: 10.1016/J.JBC.2023.104630
Page generated: Mon Aug 12 23:33:03 2024

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