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Chlorine in PDB 1nyy: Crystal Structure of the Complex Between M182T Mutant of Tem-1 and A Boronic Acid Inhibitor (105)

Enzymatic activity of Crystal Structure of the Complex Between M182T Mutant of Tem-1 and A Boronic Acid Inhibitor (105)

All present enzymatic activity of Crystal Structure of the Complex Between M182T Mutant of Tem-1 and A Boronic Acid Inhibitor (105):
3.5.2.6;

Protein crystallography data

The structure of Crystal Structure of the Complex Between M182T Mutant of Tem-1 and A Boronic Acid Inhibitor (105), PDB code: 1nyy 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) 17.00 / 1.90
Space group P 21 21 21
Cell size a, b, c (Å), α, β, γ (°) 41.498, 61.953, 89.065, 90.00, 90.00, 90.00
R / Rfree (%) 19.4 / 23

Chlorine Binding Sites:

The binding sites of Chlorine atom in the Crystal Structure of the Complex Between M182T Mutant of Tem-1 and A Boronic Acid Inhibitor (105) (pdb code 1nyy). This binding sites where shown within 5.0 Angstroms radius around Chlorine atom.
In total only one binding site of Chlorine was determined in the Crystal Structure of the Complex Between M182T Mutant of Tem-1 and A Boronic Acid Inhibitor (105), PDB code: 1nyy:

Chlorine binding site 1 out of 1 in 1nyy

Go back to Chlorine Binding Sites List in 1nyy
Chlorine binding site 1 out of 1 in the Crystal Structure of the Complex Between M182T Mutant of Tem-1 and A Boronic Acid Inhibitor (105)


Mono view


Stereo pair view

A full contact list of Chlorine with other atoms in the Cl binding site number 1 of Crystal Structure of the Complex Between M182T Mutant of Tem-1 and A Boronic Acid Inhibitor (105) within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Cl300

b:49.8
occ:0.75
 CL1 A:105300 0.0 49.8 0.8
C14 A:105300 1.7 44.2 0.8
C15 A:105300 2.7 44.3 0.8
C13 A:105300 2.7 43.3 0.8
C12 A:105300 3.1 43.0 0.8
O A:HOH511 3.1 31.8 0.5
N11 A:105300 3.2 42.8 0.8
CB A:ALA237 3.6 21.9 1.0
CE A:MET272 3.9 38.0 1.0
C7 A:105300 4.0 38.8 0.8
C16 A:105300 4.0 44.2 0.8
C18 A:105300 4.1 44.7 0.8
O10 A:105300 4.3 40.4 0.8
C8 A:105300 4.5 40.8 0.8
C17 A:105300 4.6 44.1 0.8
O A:HOH511 4.6 36.2 0.5
N4 A:105300 4.8 33.4 0.8
C5 A:105300 4.9 36.9 0.8

Reference:

X.Wang, G.Minasov, J.Blazquez, 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
Page generated: Thu Jul 10 18:34:37 2025

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