Atomistry » Potassium » PDB 2fxi-2hw8 » 2hdu
Atomistry »
  Potassium »
    PDB 2fxi-2hw8 »
      2hdu »

Potassium in PDB 2hdu: Ampc Beta-Lactamase in Complex with 2-Acetamidothiophene-3-Carboxylic Acid

Enzymatic activity of Ampc Beta-Lactamase in Complex with 2-Acetamidothiophene-3-Carboxylic Acid

All present enzymatic activity of Ampc Beta-Lactamase in Complex with 2-Acetamidothiophene-3-Carboxylic Acid:
3.5.2.6;

Protein crystallography data

The structure of Ampc Beta-Lactamase in Complex with 2-Acetamidothiophene-3-Carboxylic Acid, PDB code: 2hdu was solved by K.Babaoglu, B.K.Shoichet, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 87.04 / 1.49
Space group C 1 2 1
Cell size a, b, c (Å), α, β, γ (°) 117.905, 77.057, 97.520, 90.00, 116.86, 90.00
R / Rfree (%) 13.5 / 16.8

Potassium Binding Sites:

The binding sites of Potassium atom in the Ampc Beta-Lactamase in Complex with 2-Acetamidothiophene-3-Carboxylic Acid (pdb code 2hdu). 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 Ampc Beta-Lactamase in Complex with 2-Acetamidothiophene-3-Carboxylic Acid, PDB code: 2hdu:

Potassium binding site 1 out of 1 in 2hdu

Go back to Potassium Binding Sites List in 2hdu
Potassium binding site 1 out of 1 in the Ampc Beta-Lactamase in Complex with 2-Acetamidothiophene-3-Carboxylic Acid


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 in Complex with 2-Acetamidothiophene-3-Carboxylic Acid within 5.0Å range:
probe atom residue distance (Å) B Occ
B:K2001

b:18.9
occ:1.00
O B:HOH2256 3.0 26.3 1.0
O A:HOH1228 3.1 26.3 1.0
O B:HOH2384 3.3 34.0 1.0
CA B:PRO303 3.6 10.4 1.0
CA A:PRO303 3.6 10.9 1.0
CD A:PRO304 3.9 11.7 1.0
CA B:THR302 3.9 11.5 1.0
CG2 B:THR302 3.9 15.4 1.0
CD B:PRO304 4.0 11.9 1.0
CA A:THR302 4.0 11.9 1.0
CG2 A:THR302 4.0 15.3 1.0
O B:ILE301 4.2 11.8 1.0
O B:HOH2490 4.2 24.6 1.0
CB A:PRO303 4.2 11.8 1.0
CB B:PRO303 4.2 10.2 1.0
O A:HOH1478 4.3 18.1 0.5
CB B:THR302 4.3 12.2 1.0
O A:ILE301 4.3 11.1 1.0
N B:PRO303 4.3 10.3 1.0
N A:PRO303 4.4 10.9 1.0
CB A:THR302 4.4 13.1 1.0
OG1 B:THR302 4.4 16.4 1.0
OG1 A:THR302 4.4 17.1 1.0
C B:THR302 4.5 10.0 1.0
C B:PRO303 4.6 10.6 1.0
C A:PRO303 4.6 10.7 1.0
N A:PRO304 4.6 10.6 1.0
N B:PRO304 4.6 11.3 1.0
C A:THR302 4.6 10.5 1.0
O A:HOH1290 4.7 40.7 1.0
O B:HOH2231 4.8 27.1 1.0
CG A:PRO304 4.8 11.9 1.0
N B:THR302 4.9 11.1 1.0
O A:HOH1239 4.9 29.1 1.0
CG B:PRO304 4.9 13.8 1.0
C B:ILE301 4.9 11.2 1.0
N A:THR302 5.0 11.0 1.0

Reference:

K.Babaoglu, B.K.Shoichet. Deconstructing Fragment-Based Inhibitor Discovery Nat.Chem.Biol. V. 2 720 2006.
ISSN: ISSN 1552-4450
PubMed: 17072304
DOI: 10.1038/NCHEMBIO831
Page generated: Sun Dec 13 23:10:10 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