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Zinc in PDB 4oqg: Crystal Structure of Tem-1 Beta-Lactamase in Complex with Boron-Based Inhibitor EC25

Enzymatic activity of Crystal Structure of Tem-1 Beta-Lactamase in Complex with Boron-Based Inhibitor EC25

All present enzymatic activity of Crystal Structure of Tem-1 Beta-Lactamase in Complex with Boron-Based Inhibitor EC25:
3.5.2.6;

Protein crystallography data

The structure of Crystal Structure of Tem-1 Beta-Lactamase in Complex with Boron-Based Inhibitor EC25, PDB code: 4oqg was solved by E.Dellus-Gur, M.Elias, J.S.Fraser, D.S.Tawfik, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 45.81 / 2.40
Space group P 43 21 2
Cell size a, b, c (Å), α, β, γ (°) 81.690, 81.690, 497.920, 90.00, 90.00, 90.00
R / Rfree (%) 20.3 / 26.4

Zinc Binding Sites:

The binding sites of Zinc atom in the Crystal Structure of Tem-1 Beta-Lactamase in Complex with Boron-Based Inhibitor EC25 (pdb code 4oqg). 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 Crystal Structure of Tem-1 Beta-Lactamase in Complex with Boron-Based Inhibitor EC25, PDB code: 4oqg:

Zinc binding site 1 out of 1 in 4oqg

Go back to Zinc Binding Sites List in 4oqg
Zinc binding site 1 out of 1 in the Crystal Structure of Tem-1 Beta-Lactamase in Complex with Boron-Based Inhibitor EC25


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 1 of Crystal Structure of Tem-1 Beta-Lactamase in Complex with Boron-Based Inhibitor EC25 within 5.0Å range:
probe atom residue distance (Å) B Occ
B:Zn302

b:1.0
occ:0.50
ND1 B:HIS96 3.0 83.7 1.0
CE1 B:HIS96 3.5 85.7 1.0
O B:HOH407 3.9 32.2 1.0
CG B:HIS96 4.2 81.8 1.0
N B:HIS96 4.3 83.4 1.0
CA B:ILE95 4.5 68.7 1.0
O B:ARG94 4.6 69.6 1.0
N B:ILE95 4.6 63.7 1.0
CB B:HIS96 4.7 72.0 1.0
C B:ARG94 4.7 64.7 1.0
C B:ILE95 4.7 70.8 1.0
NE2 B:HIS96 4.8 89.3 1.0

Reference:

E.Dellus-Gur, M.Elias, E.Caselli, F.Prati, J.S.Fraser, D.S.Tawfik. Negative Epistasis in Enzyme Evolution the Thin Line Between Conformational Freedom and Anarchy To Be Published.
Page generated: Sun Oct 27 03:56:47 2024

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