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Zinc in PDB 1dxk: Metallo-Beta-Lactamase From Bacillus Cereus 569/H/9 C168S Mutant

Enzymatic activity of Metallo-Beta-Lactamase From Bacillus Cereus 569/H/9 C168S Mutant

All present enzymatic activity of Metallo-Beta-Lactamase From Bacillus Cereus 569/H/9 C168S Mutant:
3.5.2.6;

Protein crystallography data

The structure of Metallo-Beta-Lactamase From Bacillus Cereus 569/H/9 C168S Mutant, PDB code: 1dxk was solved by L.Chantalat, E.Duee, O.Dideberg, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 8.00 / 1.85
Space group C 1 2 1
Cell size a, b, c (Å), α, β, γ (°) 52.790, 61.250, 69.280, 90.00, 92.93, 90.00
R / Rfree (%) 20.5 / 26.1

Zinc Binding Sites:

The binding sites of Zinc atom in the Metallo-Beta-Lactamase From Bacillus Cereus 569/H/9 C168S Mutant (pdb code 1dxk). 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 Metallo-Beta-Lactamase From Bacillus Cereus 569/H/9 C168S Mutant, PDB code: 1dxk:

Zinc binding site 1 out of 1 in 1dxk

Go back to Zinc Binding Sites List in 1dxk
Zinc binding site 1 out of 1 in the Metallo-Beta-Lactamase From Bacillus Cereus 569/H/9 C168S Mutant


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 1 of Metallo-Beta-Lactamase From Bacillus Cereus 569/H/9 C168S Mutant within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Zn228

b:16.1
occ:1.00
NE2 A:HIS149 2.0 14.2 1.0
ND1 A:HIS88 2.1 14.2 1.0
NE2 A:HIS86 2.1 6.2 1.0
O A:HOH2232 2.3 18.6 1.0
O A:HOH2097 3.0 21.3 1.0
CE1 A:HIS149 3.0 15.1 1.0
CG A:HIS88 3.1 14.5 1.0
CD2 A:HIS149 3.1 13.0 1.0
CD2 A:HIS86 3.1 5.6 1.0
CE1 A:HIS86 3.1 3.5 1.0
CE1 A:HIS88 3.1 14.1 1.0
CB A:HIS88 3.3 13.9 1.0
OG A:SER168 3.9 10.6 1.0
O2 A:BCT230 4.0 33.9 1.0
CB A:SER168 4.1 9.5 1.0
ND1 A:HIS149 4.2 10.8 1.0
ND1 A:HIS86 4.2 5.4 1.0
CG A:HIS86 4.2 4.6 1.0
CG A:HIS149 4.2 12.5 1.0
CD2 A:HIS88 4.2 13.8 1.0
NE2 A:HIS88 4.2 13.5 1.0
C A:BCT230 4.3 33.5 1.0
O1 A:BCT230 4.4 34.1 1.0
CG2 A:THR150 4.4 8.0 1.0
OD1 A:ASP90 4.4 30.5 1.0
CA A:HIS88 4.8 14.9 1.0

Reference:

L.Chantalat, E.Duee, M.Galleni, J.M.Frere, O.Dideberg. Structural Effects of the Active Site Mutation Cysteine to Serine in Bacillus Cereus Zinc-Beta-Lactamase. Protein Sci. V. 9 1402 2000.
ISSN: ISSN 0961-8368
PubMed: 10933508
DOI: 10.1110/PS.9.7.1402
Page generated: Wed Dec 16 02:47:34 2020

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