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 / R_free (%)*	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: Thu Jul 10 17:36:26 2025

Last articles

Mn in 9LJU
Mn in 9LJW
Mn in 9LJS
Mn in 9LJR
Mn in 9LJT
Mn in 9LJV
Mg in 9UA2
Mg in 9R96
Mg in 9VM1
Mg in 9P01

	© Copyright 2008-2020 by atomistry.com
Home \| Site Map \| Copyright \| Contact us \| Privacy