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Zinc in PDB 2v20: Structure of A Tem-1 Beta-Lactamase Insertant Allosterically Regulated By Kanamycin and Anions. Complex with Sulfate.

Enzymatic activity of Structure of A Tem-1 Beta-Lactamase Insertant Allosterically Regulated By Kanamycin and Anions. Complex with Sulfate.

All present enzymatic activity of Structure of A Tem-1 Beta-Lactamase Insertant Allosterically Regulated By Kanamycin and Anions. Complex with Sulfate.:
3.5.2.6;

Protein crystallography data

The structure of Structure of A Tem-1 Beta-Lactamase Insertant Allosterically Regulated By Kanamycin and Anions. Complex with Sulfate., PDB code: 2v20 was solved by C.Evrard, H.Barrios, P.Mathonet, P.Soumillion, J.Fastrez, J.P.Declercq, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 51.50 / 1.67
Space group P 21 21 21
Cell size a, b, c (Å), α, β, γ (°) 46.080, 72.142, 73.495, 90.00, 90.00, 90.00
R / Rfree (%) 18 / 22.3

Zinc Binding Sites:

The binding sites of Zinc atom in the Structure of A Tem-1 Beta-Lactamase Insertant Allosterically Regulated By Kanamycin and Anions. Complex with Sulfate. (pdb code 2v20). This binding sites where shown within 5.0 Angstroms radius around Zinc atom.
In total only one binding site of Zinc was determined in the Structure of A Tem-1 Beta-Lactamase Insertant Allosterically Regulated By Kanamycin and Anions. Complex with Sulfate., PDB code: 2v20:

Zinc binding site 1 out of 1 in 2v20

Go back to Zinc Binding Sites List in 2v20
Zinc binding site 1 out of 1 in the Structure of A Tem-1 Beta-Lactamase Insertant Allosterically Regulated By Kanamycin and Anions. Complex with Sulfate.


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 1 of Structure of A Tem-1 Beta-Lactamase Insertant Allosterically Regulated By Kanamycin and Anions. Complex with Sulfate. within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Zn1270

b:20.1
occ:1.00
 ND1 A:HIS138 2.0 14.7 1.0
ND1 A:HIS133 2.2 21.8 1.0
O A:HOH2273 2.4 20.8 1.0
CE1 A:HIS138 2.9 12.6 1.0
CG A:HIS138 3.1 10.9 1.0
CE1 A:HIS133 3.1 22.2 1.0
CG A:HIS133 3.1 21.2 1.0
CB A:HIS133 3.5 18.6 1.0
CB A:HIS138 3.5 12.0 1.0
CA A:HIS138 3.9 13.6 1.0
NE2 A:HIS138 4.1 14.3 1.0
NE2 A:HIS133 4.1 25.9 1.0
CD2 A:HIS138 4.1 15.2 1.0
CD2 A:HIS133 4.2 25.4 1.0
CA A:HIS133 4.3 16.9 1.0
O A:HIS138 4.7 16.1 1.0
C A:HIS138 4.9 15.0 1.0
O A:HOH2073 4.9 42.2 1.0
O A:HIS133 4.9 17.3 1.0
C A:HIS133 4.9 18.0 1.0
N A:HIS138 5.0 12.9 1.0

Reference:

A.N.Volkov, H.Barrios, P.Mathonet, C.Evrard, M.Ubbink, J.P.Declercq, P.Soumillion, J.Fastrez. Engineering An Allosteric Binding Site For Aminoglycosides Into TEM1-Beta-Lactamase. Chembiochem V. 12 904 2011.
ISSN: ISSN 1439-4227
PubMed: 21425229
DOI: 10.1002/CBIC.201000568
Page generated: Thu Oct 17 04:06:08 2024

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