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Zinc in PDB 2nxa: Structure of Zn-Dependent Metallo-Beta-Lactamase From Bacillus Cereus R121H, C221D Double Mutant

Enzymatic activity of Structure of Zn-Dependent Metallo-Beta-Lactamase From Bacillus Cereus R121H, C221D Double Mutant

All present enzymatic activity of Structure of Zn-Dependent Metallo-Beta-Lactamase From Bacillus Cereus R121H, C221D Double Mutant:
3.5.2.6;

Protein crystallography data

The structure of Structure of Zn-Dependent Metallo-Beta-Lactamase From Bacillus Cereus R121H, C221D Double Mutant, PDB code: 2nxa 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 / 2.29
Space group C 1 2 1
Cell size a, b, c (Å), α, β, γ (°) 52.471, 61.008, 68.674, 90.00, 92.85, 90.00
R / Rfree (%) 16.3 / 25.6

Zinc Binding Sites:

The binding sites of Zinc atom in the Structure of Zn-Dependent Metallo-Beta-Lactamase From Bacillus Cereus R121H, C221D Double Mutant (pdb code 2nxa). 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 Zn-Dependent Metallo-Beta-Lactamase From Bacillus Cereus R121H, C221D Double Mutant, PDB code: 2nxa:

Zinc binding site 1 out of 1 in 2nxa

Go back to Zinc Binding Sites List in 2nxa
Zinc binding site 1 out of 1 in the Structure of Zn-Dependent Metallo-Beta-Lactamase From Bacillus Cereus R121H, C221D Double Mutant


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 1 of Structure of Zn-Dependent Metallo-Beta-Lactamase From Bacillus Cereus R121H, C221D Double Mutant within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Zn301

b:30.4
occ:1.00
 NE2 A:HIS149 2.1 13.2 1.0
ND1 A:HIS88 2.2 20.9 1.0
NE2 A:HIS86 2.2 15.9 1.0
CE1 A:HIS86 3.1 16.3 1.0
CD2 A:HIS149 3.1 13.5 1.0
CD2 A:HIS86 3.1 14.9 1.0
CE1 A:HIS149 3.1 11.2 1.0
CE1 A:HIS88 3.2 23.2 1.0
CG A:HIS88 3.2 20.4 1.0
CB A:HIS88 3.4 21.8 1.0
OD1 A:ASP168 3.7 29.6 1.0
O A:HOH394 4.1 18.1 1.0
ND1 A:HIS86 4.1 16.9 1.0
CG A:ASP168 4.2 21.8 1.0
CG A:HIS86 4.2 15.9 1.0
CB A:ASP168 4.2 19.4 1.0
ND1 A:HIS149 4.2 12.6 1.0
CG A:HIS149 4.3 12.5 1.0
OD2 A:ASP90 4.3 46.3 1.0
CG2 A:THR150 4.3 8.3 1.0
NE2 A:HIS88 4.3 23.1 1.0
CD2 A:HIS88 4.3 16.3 1.0
OD1 A:ASP90 4.4 43.6 1.0
CD2 A:HIS91 4.6 31.5 1.0
CG A:ASP90 4.7 37.4 1.0
NE2 A:HIS91 4.8 33.3 1.0
CA A:HIS88 4.9 22.6 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: Thu Oct 17 02:22:41 2024

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