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Chlorine in PDB 1jwz: Crystal Structure of Tem-64 Beta-Lactamase in Complex with A Boronic Acid Inhibitor (105)

Enzymatic activity of Crystal Structure of Tem-64 Beta-Lactamase in Complex with A Boronic Acid Inhibitor (105)

All present enzymatic activity of Crystal Structure of Tem-64 Beta-Lactamase in Complex with A Boronic Acid Inhibitor (105):
3.5.2.6;

Protein crystallography data

The structure of Crystal Structure of Tem-64 Beta-Lactamase in Complex with A Boronic Acid Inhibitor (105), PDB code: 1jwz 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) 19.00 / 1.80
Space group P 21 21 21
Cell size a, b, c (Å), α, β, γ (°) 72.002, 34.546, 105.489, 90.00, 90.00, 90.00
R / Rfree (%) 16.8 / 18.9

Chlorine Binding Sites:

The binding sites of Chlorine atom in the Crystal Structure of Tem-64 Beta-Lactamase in Complex with A Boronic Acid Inhibitor (105) (pdb code 1jwz). 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 Tem-64 Beta-Lactamase in Complex with A Boronic Acid Inhibitor (105), PDB code: 1jwz:

Chlorine binding site 1 out of 1 in 1jwz

Go back to Chlorine Binding Sites List in 1jwz
Chlorine binding site 1 out of 1 in the Crystal Structure of Tem-64 Beta-Lactamase in Complex with 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 Tem-64 Beta-Lactamase in Complex with A Boronic Acid Inhibitor (105) within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Cl300

b:38.6
occ:1.00
 CL1 A:105300 0.0 38.6 1.0
C14 A:105300 1.7 33.4 1.0
C15 A:105300 2.7 32.4 1.0
C13 A:105300 2.8 30.9 1.0
C12 A:105300 3.1 27.5 1.0
CE A:MET272 3.2 29.5 1.0
N11 A:105300 3.3 26.9 1.0
CB A:ALA237 3.9 14.5 1.0
O A:HOH588 3.9 39.9 1.0
C16 A:105300 4.1 30.4 1.0
C7 A:105300 4.1 23.9 1.0
C18 A:105300 4.1 29.9 1.0
O10 A:105300 4.4 27.8 1.0
O A:HOH589 4.5 38.9 1.0
O A:HOH571 4.5 32.6 1.0
O6 A:105300 4.6 18.2 1.0
C17 A:105300 4.6 29.9 1.0
C8 A:105300 4.6 24.5 1.0
SD A:MET272 4.7 30.2 1.0
C5 A:105300 4.9 20.2 1.0

Reference:

X.Wang, G.Minasov, B.K.Shoichet. Evolution of An Antibiotic Resistance Enzyme Constrained By Stability and Activity Trade-Offs. J.Mol.Biol. V. 320 85 2002.
ISSN: ISSN 0022-2836
PubMed: 12079336
DOI: 10.1016/S0022-2836(02)00400-X
Page generated: Fri Jul 19 23:06:04 2024

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