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Zinc in PDB 2v1z: Structure of A Tem-1 Beta-Lactamase Insertant Allosterically Regulated By Kanamycin and Anions.

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

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

Protein crystallography data

The structure of Structure of A Tem-1 Beta-Lactamase Insertant Allosterically Regulated By Kanamycin and Anions., PDB code: 2v1z 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) 52.41 / 1.60
Space group P 21 21 21
Cell size a, b, c (Å), α, β, γ (°) 47.113, 70.609, 78.313, 90.00, 90.00, 90.00
R / Rfree (%) 16.9 / 20.6

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. (pdb code 2v1z). 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., PDB code: 2v1z:

Zinc binding site 1 out of 1 in 2v1z

Go back to Zinc Binding Sites List in 2v1z
Zinc binding site 1 out of 1 in the Structure of A Tem-1 Beta-Lactamase Insertant Allosterically Regulated By Kanamycin and Anions.


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. within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Zn1271

b:18.1
occ:1.00
 ND1 A:HIS133 2.0 14.1 1.0
ND1 A:HIS138 2.1 17.7 1.0
O A:HOH2352 2.2 6.9 1.0
CE1 A:HIS133 2.9 18.0 1.0
CE1 A:HIS138 3.0 14.5 1.0
CG A:HIS133 3.1 13.8 1.0
CG A:HIS138 3.2 14.0 1.0
CB A:HIS133 3.5 14.1 1.0
CB A:HIS138 3.5 15.0 1.0
CA A:HIS138 4.0 14.6 1.0
NE2 A:HIS133 4.1 17.2 1.0
CD2 A:HIS133 4.1 15.4 1.0
NE2 A:HIS138 4.2 16.3 1.0
CD2 A:HIS138 4.2 15.7 1.0
CA A:HIS133 4.5 14.4 1.0
O A:HIS138 4.5 16.6 1.0
C A:HIS138 4.7 15.6 1.0
O A:HOH2087 4.9 36.0 1.0
O A:HOH2083 4.9 26.4 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: Wed Dec 16 03:54:22 2020

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