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Zinc in PDB 2nzf: Structure of Beta-Lactamase II From Bacillus Cereus. R121H, C221S Double Mutant. Space Group C2.

Enzymatic activity of Structure of Beta-Lactamase II From Bacillus Cereus. R121H, C221S Double Mutant. Space Group C2.

All present enzymatic activity of Structure of Beta-Lactamase II From Bacillus Cereus. R121H, C221S Double Mutant. Space Group C2.:
3.5.2.6;

Protein crystallography data

The structure of Structure of Beta-Lactamase II From Bacillus Cereus. R121H, C221S Double Mutant. Space Group C2., PDB code: 2nzf was solved by F.J.Medrano Martin, A.J.Vila, J.M.Gonzalez, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 68.52 / 2.28
Space group C 1 2 1
Cell size a, b, c (Å), α, β, γ (°) 52.587, 61.156, 68.634, 90.00, 93.11, 90.00
R / Rfree (%) 16.3 / 23.8

Zinc Binding Sites:

The binding sites of Zinc atom in the Structure of Beta-Lactamase II From Bacillus Cereus. R121H, C221S Double Mutant. Space Group C2. (pdb code 2nzf). 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 Beta-Lactamase II From Bacillus Cereus. R121H, C221S Double Mutant. Space Group C2., PDB code: 2nzf:

Zinc binding site 1 out of 1 in 2nzf

Go back to Zinc Binding Sites List in 2nzf
Zinc binding site 1 out of 1 in the Structure of Beta-Lactamase II From Bacillus Cereus. R121H, C221S Double Mutant. Space Group C2.


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 1 of Structure of Beta-Lactamase II From Bacillus Cereus. R121H, C221S Double Mutant. Space Group C2. within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Zn228

b:21.4
occ:1.00
ND1 A:HIS88 2.0 14.2 1.0
NE2 A:HIS149 2.1 11.9 1.0
NE2 A:HIS86 2.2 10.9 1.0
CE1 A:HIS88 3.0 17.2 1.0
CE1 A:HIS149 3.0 11.1 1.0
CG A:HIS88 3.0 14.1 1.0
CD2 A:HIS86 3.1 11.0 1.0
CE1 A:HIS86 3.1 12.8 1.0
CD2 A:HIS149 3.1 11.8 1.0
O A:HOH346 3.3 33.1 1.0
CB A:HIS88 3.4 15.5 1.0
OD1 A:ASP90 4.0 22.2 1.0
NE2 A:HIS88 4.1 14.3 1.0
ND1 A:HIS149 4.1 11.8 1.0
CD2 A:HIS88 4.2 13.4 1.0
ND1 A:HIS86 4.2 12.0 1.0
CG2 A:THR150 4.2 4.3 1.0
CG A:HIS86 4.2 13.3 1.0
OG A:SER168 4.2 11.4 1.0
CG A:HIS149 4.2 10.7 1.0
CB A:SER168 4.3 12.9 1.0
CD2 A:HIS91 4.5 17.9 1.0
NE2 A:HIS91 4.8 18.6 1.0
CA A:HIS88 4.8 16.1 1.0
OD2 A:ASP90 4.9 24.4 1.0
CG A:ASP90 4.9 20.5 1.0
O A:HOH229 4.9 15.6 1.0
O A:HOH340 4.9 23.1 1.0

Reference:

J.M.Gonzalez, F.J.Medrano Martin, A.L.Costello, D.L.Tierney, A.J.Vila. The ZN2 Position in Metallo-Beta-Lactamases Is Critical For Activity: A Study on Chimeric Metal Sites on A Conserved Protein Scaffold. J.Mol.Biol. V. 373 1141 2007.
ISSN: ISSN 0022-2836
PubMed: 17915249
DOI: 10.1016/J.JMB.2007.08.031
Page generated: Wed Dec 16 03:45:01 2020

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