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

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

The structure of Crystal Structure of the Complex Between M182T Mutant of Tem-1 and A Boronic Acid Inhibitor (Cxb), PDB code: 1nym 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 / 1.20
Space group	P 21 21 21
Cell size a, b, c (Å), α, β, γ (°)	41.344, 61.659, 89.129, 90.00, 90.00, 90.00
R / Rfree (%)	n/a / 14.8

The binding sites of Potassium atom in the Crystal Structure of the Complex Between M182T Mutant of Tem-1 and A Boronic Acid Inhibitor (Cxb) (pdb code 1nym). This binding sites where shown within 5.0 Angstroms radius around Potassium atom.
In total 3 binding sites of Potassium where determined in the Crystal Structure of the Complex Between M182T Mutant of Tem-1 and A Boronic Acid Inhibitor (Cxb), PDB code: 1nym:
Jump to Potassium binding site number: 1; 2; 3;

Potassium binding site 1 out of 3 in the Crystal Structure of the Complex Between M182T Mutant of Tem-1 and A Boronic Acid Inhibitor (Cxb)


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 (Cxb) within 5.0Å range: probe atom residue distance (Å) B Occ A:K1000 b:16.9 occ:0.56 OE2 A:GLU58 2.9 13.1 0.6 O A:LEU57 2.9 13.0 1.0 OE1 A:GLU58 3.0 12.6 0.4 O A:HOH1653 3.1 22.3 0.4 O A:HOH1583 3.4 22.1 1.0 CD A:GLU58 3.6 12.9 0.4 CD A:GLU58 3.7 12.3 0.6 O A:HOH1532 3.7 14.4 1.0 OE2 A:GLU58 3.8 14.4 0.4 C A:LEU57 3.9 10.9 1.0 OE1 A:GLU58 4.0 11.3 0.6 CA A:GLU58 4.2 9.8 0.4 CA A:GLU58 4.3 10.0 0.6 O A:HOH1515 4.3 16.1 1.0 N A:GLU58 4.4 10.2 0.6 N A:GLU58 4.5 10.6 0.4 CG A:GLU58 4.7 11.9 0.4 O A:HOH1653 4.7 14.4 0.6 CG A:GLU58 4.7 12.0 0.6 CB A:GLU58 4.9 10.7 0.4 CB A:GLU58 4.9 11.5 0.6 CA A:LEU57 5.0 10.5 1.0

Potassium binding site 2 out of 3 in the Crystal Structure of the Complex Between M182T Mutant of Tem-1 and A Boronic Acid Inhibitor (Cxb)


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 the Complex Between M182T Mutant of Tem-1 and A Boronic Acid Inhibitor (Cxb) within 5.0Å range: probe atom residue distance (Å) B Occ A:K1001 b:14.0 occ:0.47 O A:TYR97 2.6 15.3 1.0 O A:LEU113 2.7 15.2 1.0 O A:HOH1593 2.9 22.7 1.0 O A:HOH1691 3.2 35.2 1.0 O A:HOH1681 3.3 23.1 0.5 O A:HOH1581 3.5 25.3 1.0 C A:TYR97 3.7 12.5 1.0 C A:LEU113 3.8 12.2 1.0 O A:HOH1693 4.2 28.1 1.0 CA A:SER98 4.3 12.4 0.5 O A:THR114 4.3 15.1 1.0 OG A:SER98 4.3 12.6 0.5 CB A:SER98 4.3 12.0 0.5 CA A:SER98 4.4 13.7 0.5 N A:TYR97 4.4 12.6 1.0 N A:SER98 4.5 11.7 0.5 N A:SER98 4.5 11.6 0.5 CA A:THR114 4.6 14.6 1.0 N A:THR114 4.7 12.4 1.0 CA A:LEU113 4.7 13.1 1.0 C A:THR114 4.7 13.2 1.0 CA A:TYR97 4.7 11.3 1.0 O A:HOH1603 4.7 22.7 1.0 CB A:LEU113 4.9 14.5 1.0 CB A:SER98 5.0 12.6 0.5

Potassium binding site 3 out of 3 in the Crystal Structure of the Complex Between M182T Mutant of Tem-1 and A Boronic Acid Inhibitor (Cxb)


Mono view


Stereo pair view

A full contact list of Potassium with other atoms in the K binding site number 3 of Crystal Structure of the Complex Between M182T Mutant of Tem-1 and A Boronic Acid Inhibitor (Cxb) within 5.0Å range: probe atom residue distance (Å) B Occ A:K1003 b:14.8 occ:0.49 CB A:ASP214 1.3 10.1 0.5 CG A:ASP214 2.0 10.9 0.5 CA A:ASP214 2.4 12.0 0.5 O A:ASP233 2.6 10.0 1.0 OD2 A:ASP214 2.6 11.7 0.5 O A:MET211 2.6 11.2 1.0 O A:ALA213 2.7 15.7 0.5 N A:ASP214 2.9 12.3 0.5 OD1 A:ASP214 2.9 12.8 0.5 OD1 A:ASP233 2.9 12.2 1.0 C A:MET211 3.5 9.5 1.0 C A:ASP233 3.5 8.9 1.0 C A:ASP214 3.7 11.7 0.5 CA A:MET211 3.8 9.9 1.0 C A:ALA213 3.8 12.7 0.5 CB A:ASP214 3.8 14.4 0.5 NH2 A:ARG222 4.0 12.4 1.0 O A:TRP210 4.0 11.6 1.0 CG A:ASP233 4.1 10.8 1.0 N A:ASP233 4.1 9.1 1.0 CA A:ASP214 4.1 12.9 0.5 C A:ALA213 4.2 12.3 0.5 O A:ASP214 4.2 14.8 0.5 OD2 A:ASP214 4.2 16.7 0.5 O A:ILE127 4.3 13.5 1.0 CA A:ASP233 4.3 9.4 1.0 N A:LYS234 4.4 9.3 1.0 N A:ASP214 4.4 14.6 0.5 CG A:ASP214 4.5 14.2 0.5 CG2 A:ILE127 4.5 10.9 1.0 N A:LYS215 4.6 11.9 0.5 CA A:LYS234 4.6 8.9 1.0 N A:GLU212 4.6 11.2 0.5 N A:GLU212 4.6 11.3 0.5 N A:ALA213 4.7 11.8 0.5 CB A:MET211 4.7 10.2 1.0 O A:HOH1543 4.7 15.2 1.0 N A:ALA213 4.7 12.6 0.5 C A:GLU212 4.8 11.1 0.5 C A:GLU212 4.8 11.3 0.5 CB A:ASP233 4.8 9.9 1.0 N A:MET211 4.8 11.0 1.0 CA A:THR128 4.8 12.5 0.6 O A:ALA213 4.9 13.2 0.5 C A:TRP210 4.9 10.7 1.0 CA A:ALA213 4.9 12.5 0.5 CZ A:ARG222 4.9 12.1 1.0 CA A:THR128 4.9 12.7 0.4 C A:ILE127 4.9 11.1 1.0

X.Wang, G.Minasov, 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