Potassium in PDB 2p74: Ctx-M-9 Class A Beta-Lactamase Apo Crystal Structure at 0.88 Angstrom Resolution

All present enzymatic activity of Ctx-M-9 Class A Beta-Lactamase Apo Crystal Structure at 0.88 Angstrom Resolution:
3.5.2.6;

The structure of Ctx-M-9 Class A Beta-Lactamase Apo Crystal Structure at 0.88 Angstrom Resolution, PDB code: 2p74 was solved by Y.Chen, R.Bonnet, B.K.Shoichet, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	10.00 / 0.88
Space group	P 1 21 1
Cell size a, b, c (Å), α, β, γ (°)	45.162, 106.796, 47.785, 90.00, 102.09, 90.00
R / Rfree (%)	10 / 11.4

The binding sites of Potassium atom in the Ctx-M-9 Class A Beta-Lactamase Apo Crystal Structure at 0.88 Angstrom Resolution (pdb code 2p74). This binding sites where shown within 5.0 Angstroms radius around Potassium atom.
In total 2 binding sites of Potassium where determined in the Ctx-M-9 Class A Beta-Lactamase Apo Crystal Structure at 0.88 Angstrom Resolution, PDB code: 2p74:
Jump to Potassium binding site number: 1; 2;

Potassium binding site 1 out of 2 in the Ctx-M-9 Class A Beta-Lactamase Apo Crystal Structure at 0.88 Angstrom Resolution


Mono view


Stereo pair view

A full contact list of Potassium with other atoms in the K binding site number 1 of Ctx-M-9 Class A Beta-Lactamase Apo Crystal Structure at 0.88 Angstrom Resolution within 5.0Å range: probe atom residue distance (Å) B Occ A:K1006 b:6.1 occ:0.49 O A:HOH2960 0.8 19.2 0.5 O2 A:PO41001 2.7 7.3 0.1 HG A:SER130 2.7 10.2 1.0 O A:HOH2078 2.8 12.7 1.0 O A:SER130 2.8 6.8 1.0 OG A:SER130 2.9 6.8 1.0 OG A:SER70 2.9 7.3 1.0 O2 A:PO41001 2.9 6.3 0.5 OD1 A:ASN132 3.0 8.5 1.0 HG A:SER70 3.0 11.0 1.0 HB3 A:SER130 3.0 7.8 1.0 O A:HOH2645 3.1 30.5 1.0 HD21 A:ASN132 3.4 12.2 1.0 CB A:SER130 3.4 6.5 1.0 HD1 A:TYR105 3.5 13.8 1.0 HZ2 A:LYS73 3.6 11.2 1.0 CG A:ASN132 3.7 8.0 1.0 C A:SER130 3.8 5.8 1.0 O A:HOH2479 3.8 8.5 1.0 HZ1 A:LYS73 3.8 11.2 1.0 ND2 A:ASN132 3.8 10.1 1.0 HE2 A:LYS73 3.9 8.1 1.0 P A:PO41001 3.9 6.9 0.1 CB A:SER70 4.0 5.9 1.0 HB2 A:SER70 4.0 7.1 1.0 O A:HOH2226 4.0 9.6 1.0 NZ A:LYS73 4.1 7.5 1.0 CA A:SER130 4.1 6.0 1.0 P A:PO41001 4.1 6.0 0.5 HB3 A:TYR105 4.1 16.6 1.0 O1 A:PO41001 4.2 7.9 0.1 CD1 A:TYR105 4.2 11.5 1.0 HB3 A:SER70 4.2 7.1 1.0 HB2 A:SER130 4.3 7.8 1.0 HA A:SER130 4.3 7.2 1.0 O4 A:PO41001 4.4 7.6 0.5 O3 A:PO41001 4.4 6.6 0.1 O1 A:PO41001 4.4 9.0 0.5 CE A:LYS73 4.5 6.7 1.0 HD22 A:ASN132 4.6 12.2 1.0 HZ1 A:LYS234 4.6 8.9 1.0 HE1 A:TYR105 4.7 15.5 1.0 CE1 A:TYR105 4.9 12.9 1.0 CB A:TYR105 4.9 13.8 1.0 HZ3 A:LYS73 4.9 11.2 1.0 H A:ASN132 4.9 7.5 1.0 HD2 A:LYS73 5.0 7.4 1.0 N A:ASP131 5.0 5.6 1.0 O A:HOH2528 5.0 33.0 1.0

Potassium binding site 2 out of 2 in the Ctx-M-9 Class A Beta-Lactamase Apo Crystal Structure at 0.88 Angstrom Resolution


Mono view


Stereo pair view

A full contact list of Potassium with other atoms in the K binding site number 2 of Ctx-M-9 Class A Beta-Lactamase Apo Crystal Structure at 0.88 Angstrom Resolution within 5.0Å range: probe atom residue distance (Å) B Occ B:K1007 b:5.8 occ:0.47 O B:HOH2975 0.7 16.8 0.5 HG B:SER130 2.7 10.7 1.0 O4 B:PO41002 2.8 7.9 0.2 O B:SER130 2.8 7.2 1.0 O B:HOH2520 2.8 11.9 1.0 OG B:SER70 2.9 7.3 1.0 O B:HOH2748 2.9 29.0 1.0 OG B:SER130 2.9 7.2 1.0 O4 B:PO41002 2.9 6.1 0.5 OD1 B:ASN132 2.9 8.4 1.0 HB3 B:SER130 3.0 8.0 1.0 HG B:SER70 3.1 10.9 1.0 HD21 B:ASN132 3.3 11.0 1.0 HD1 B:TYR105 3.4 14.6 1.0 CB B:SER130 3.4 6.6 1.0 HZ2 B:LYS73 3.6 12.0 1.0 CG B:ASN132 3.7 7.6 1.0 O B:HOH2480 3.7 4.6 0.5 C B:SER130 3.8 6.3 1.0 ND2 B:ASN132 3.8 9.2 1.0 HZ1 B:LYS73 3.8 12.0 1.0 HE2 B:LYS73 3.8 8.1 1.0 CB B:SER70 4.0 6.1 1.0 HB2 B:SER70 4.0 7.3 1.0 P B:PO41002 4.0 7.3 0.2 O B:HOH2484 4.1 10.6 1.0 NZ B:LYS73 4.1 8.0 1.0 CD1 B:TYR105 4.1 12.2 1.0 CA B:SER130 4.1 6.1 1.0 P B:PO41002 4.1 6.6 0.5 O2 B:PO41002 4.2 9.6 0.2 HB3 B:SER70 4.2 7.3 1.0 HB2 B:SER130 4.3 8.0 1.0 HB3 B:TYR105 4.3 14.7 1.0 HA B:SER130 4.3 7.3 1.0 O2 B:PO41002 4.4 7.2 0.5 CE B:LYS73 4.5 6.7 1.0 O3 B:PO41002 4.5 9.4 0.5 HE1 B:TYR105 4.5 17.9 1.0 O B:HOH2798 4.5 27.5 0.5 O3 B:PO41002 4.6 8.9 0.2 HD22 B:ASN132 4.6 11.0 1.0 HZ1 B:LYS234 4.7 9.2 1.0 CE1 B:TYR105 4.7 14.9 1.0 H B:ASN132 4.9 7.6 1.0 HZ3 B:LYS73 4.9 12.0 1.0 CG B:TYR105 4.9 15.4 1.0 HD2 B:LYS73 4.9 7.4 1.0 N B:ASP131 4.9 6.1 1.0

Y.Chen, R.Bonnet, B.K.Shoichet. The Acylation Mechanism of Ctx-M Beta-Lactamase at 0.88 A Resolution. J.Am.Chem.Soc. V. 129 5378 2007.
ISSN: ISSN 0002-7863
PubMed: 17408273
DOI: 10.1021/JA0712064