Zinc in PDB 6tbw: Crystal Structure of Ampc From E.Coli with Avibactam

Enzymatic activity of Crystal Structure of Ampc From E.Coli with Avibactam

All present enzymatic activity of Crystal Structure of Ampc From E.Coli with Avibactam:
3.5.2.6;

Protein crystallography data

The structure of Crystal Structure of Ampc From E.Coli with Avibactam, PDB code: 6tbw was solved by P.A.Lang, T.M.Leissing, C.J.Schofield, J.Brem, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 79.72 / 1.51
Space group P 43 3 2
Cell size a, b, c (Å), α, β, γ (°) 138.083, 138.083, 138.083, 90.00, 90.00, 90.00
R / Rfree (%) 15.8 / 18.1

Other elements in 6tbw:

The structure of Crystal Structure of Ampc From E.Coli with Avibactam also contains other interesting chemical elements:

Chlorine (Cl) 1 atom

Zinc Binding Sites:

The binding sites of Zinc atom in the Crystal Structure of Ampc From E.Coli with Avibactam (pdb code 6tbw). This binding sites where shown within 5.0 Angstroms radius around Zinc atom.
In total 2 binding sites of Zinc where determined in the Crystal Structure of Ampc From E.Coli with Avibactam, PDB code: 6tbw:
Jump to Zinc binding site number: 1; 2;

Zinc binding site 1 out of 2 in 6tbw

Go back to Zinc Binding Sites List in 6tbw
Zinc binding site 1 out of 2 in the Crystal Structure of Ampc From E.Coli with Avibactam


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 Ampc From E.Coli with Avibactam within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Zn403

b:15.8
occ:0.33
NE2 A:HIS13 2.0 19.4 1.0
CL A:CL405 2.2 19.9 0.3
CD2 A:HIS13 3.0 17.0 1.0
CE1 A:HIS13 3.1 17.0 1.0
ND1 A:HIS13 4.1 15.9 1.0
CG A:HIS13 4.2 16.3 1.0

Zinc binding site 2 out of 2 in 6tbw

Go back to Zinc Binding Sites List in 6tbw
Zinc binding site 2 out of 2 in the Crystal Structure of Ampc From E.Coli with Avibactam


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 2 of Crystal Structure of Ampc From E.Coli with Avibactam within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Zn404

b:32.7
occ:0.59
O A:HOH716 2.0 38.0 0.7
NE2 A:HIS186 2.1 37.4 1.0
O A:HOH523 2.1 38.7 1.0
O A:HOH525 2.1 39.3 1.0
O A:HOH768 2.2 34.8 0.6
CE1 A:HIS186 3.1 35.7 1.0
CD2 A:HIS186 3.1 33.2 1.0
O A:HOH805 3.9 57.1 1.0
O A:HOH586 4.0 48.0 1.0
OE2 A:GLU195 4.2 47.4 1.0
ND1 A:HIS186 4.2 32.2 1.0
O A:HOH809 4.3 48.2 1.0
CG A:HIS186 4.3 29.5 1.0
OE1 A:GLU195 4.3 43.2 1.0
CD A:GLU195 4.6 46.3 1.0

Reference:

P.A.Lang, T.M.Leissing, M.G.P.Page, C.J.Schofield, J.Brem. Structural Investigations of the Inhibition of Escherichia Coli Ampc Beta-Lactamase By Diazabicyclooctanes. Antimicrob.Agents Chemother. 2020.
ISSN: ESSN 1098-6596
PubMed: 33199391
DOI: 10.1128/AAC.02073-20
Page generated: Wed Dec 16 12:52:31 2020

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