Atomistry » Potassium » PDB 1k4d-1m40 » 1li0
Atomistry »
  Potassium »
    PDB 1k4d-1m40 »
      1li0 »

Potassium in PDB 1li0: Crystal Structure of Tem-32 Beta-Lactamase at 1.6 Angstrom

Enzymatic activity of Crystal Structure of Tem-32 Beta-Lactamase at 1.6 Angstrom

All present enzymatic activity of Crystal Structure of Tem-32 Beta-Lactamase at 1.6 Angstrom:
3.5.2.6;

Protein crystallography data

The structure of Crystal Structure of Tem-32 Beta-Lactamase at 1.6 Angstrom, PDB code: 1li0 was solved by X.Wang, G.Minasov, B.K.Shoichet, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 17.00 / 1.61
Space group P 21 21 21
Cell size a, b, c (Å), α, β, γ (°) 41.222, 60.504, 88.712, 90.00, 90.00, 90.00
R / Rfree (%) 19.7 / 21.7

Potassium Binding Sites:

The binding sites of Potassium atom in the Crystal Structure of Tem-32 Beta-Lactamase at 1.6 Angstrom (pdb code 1li0). 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 Tem-32 Beta-Lactamase at 1.6 Angstrom, PDB code: 1li0:
Jump to Potassium binding site number: 1; 2;

Potassium binding site 1 out of 2 in 1li0

Go back to Potassium Binding Sites List in 1li0
Potassium binding site 1 out of 2 in the Crystal Structure of Tem-32 Beta-Lactamase at 1.6 Angstrom


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 Tem-32 Beta-Lactamase at 1.6 Angstrom within 5.0Å range:
probe atom residue distance (Å) B Occ
A:K2

b:20.9
occ:0.50
O A:HOH581 2.6 35.7 0.5
O A:HOH583 2.7 47.0 1.0
OD1 A:ASP233 2.7 25.7 1.0
O A:MET211 2.8 15.2 1.0
O A:ASP233 2.9 17.8 1.0
O A:ALA213 3.2 41.7 1.0
O A:HOH581 3.6 30.9 0.5
C A:MET211 3.7 17.8 1.0
C A:ASP233 3.7 15.4 1.0
NH2 A:ARG222 3.8 29.3 1.0
CG A:ASP233 3.8 23.0 1.0
CA A:MET211 4.2 16.7 1.0
N A:ASP233 4.3 15.1 1.0
C A:ALA213 4.4 40.0 1.0
NE A:ARG222 4.4 28.9 1.0
CA A:ASP233 4.4 16.8 1.0
CZ A:ARG222 4.5 32.6 1.0
O A:TRP210 4.5 20.1 1.0
O A:HOH337 4.5 30.9 1.0
OD2 A:ASP233 4.6 23.7 1.0
N A:LYS234 4.6 14.4 1.0
N A:GLU212 4.7 18.6 1.0
CB A:ALA217 4.7 50.8 1.0
CB A:ASP233 4.7 16.7 1.0
C A:GLU212 4.8 26.1 1.0
CA A:LYS234 4.8 14.0 1.0
N A:ALA213 4.8 29.9 1.0

Potassium binding site 2 out of 2 in 1li0

Go back to Potassium Binding Sites List in 1li0
Potassium binding site 2 out of 2 in the Crystal Structure of Tem-32 Beta-Lactamase at 1.6 Angstrom


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 Tem-32 Beta-Lactamase at 1.6 Angstrom within 5.0Å range:
probe atom residue distance (Å) B Occ
A:K3

b:27.4
occ:0.65
ND2 A:ASN100 2.1 33.1 0.3
OD1 A:ASN100 2.3 32.7 0.3
CG A:ASN100 2.5 30.7 0.3
OD1 A:ASP101 3.1 19.4 1.0
O A:HOH360 3.8 15.1 1.0
CG A:ASP101 3.8 22.6 1.0
CB A:ASN100 3.9 29.6 0.7
O A:ASN100 3.9 27.6 0.3
CB A:ASN100 4.0 30.4 0.3
O A:ASN100 4.0 28.3 0.7
C A:ASN100 4.1 27.1 0.3
O A:HOH586 4.1 20.9 1.0
C A:ASN100 4.1 27.2 0.7
OD2 A:ASP101 4.2 21.0 1.0
N A:ASP101 4.4 24.1 1.0
O A:HOH330 4.4 25.6 1.0
CA A:ASP101 4.5 23.5 1.0
O A:HOH325 4.6 20.8 1.0
CA A:ASN100 4.7 29.0 0.7
CA A:ASN100 4.7 28.9 0.3
CB A:ASP101 4.8 21.1 1.0

Reference:

X.Wang, G.Minasov, B.K.Shoichet. The Structural Bases of Antibiotic Resistance in the Clinically Derived Mutant Beta-Lactamases Tem-30, Tem-32, and Tem-34. J.Biol.Chem. V. 277 32149 2002.
ISSN: ISSN 0021-9258
PubMed: 12058046
DOI: 10.1074/JBC.M204212200
Page generated: Sun Dec 13 22:49:46 2020

Last articles

Zn in 8WB0
Zn in 8WAX
Zn in 8WAU
Zn in 8WAZ
Zn in 8WAY
Zn in 8WAV
Zn in 8WAW
Zn in 8WAT
Zn in 8W7M
Zn in 8WD3
© Copyright 2008-2020 by atomistry.com
Home   |    Site Map   |    Copyright   |    Contact us   |    Privacy