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Zinc in PDB 6t3d: Crystal Structure of Ampc From E.Coli

Enzymatic activity of Crystal Structure of Ampc From E.Coli

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

Protein crystallography data

The structure of Crystal Structure of Ampc From E.Coli, PDB code: 6t3d 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) 49.21 / 1.50
Space group P 43 3 2
Cell size a, b, c (Å), α, β, γ (°) 139.180, 139.180, 139.180, 90.00, 90.00, 90.00
R / Rfree (%) 15.8 / 17.8

Other elements in 6t3d:

The structure of Crystal Structure of Ampc From E.Coli 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 (pdb code 6t3d). 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, PDB code: 6t3d:
Jump to Zinc binding site number: 1; 2;

Zinc binding site 1 out of 2 in 6t3d

Go back to Zinc Binding Sites List in 6t3d
Zinc binding site 1 out of 2 in the Crystal Structure of Ampc From E.Coli


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 within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Zn402

b:23.6
occ:0.33
NE2 A:HIS13 2.0 23.0 1.0
CL A:CL405 2.3 29.0 0.3
CE1 A:HIS13 3.0 25.1 1.0
CD2 A:HIS13 3.0 23.2 1.0
HE1 A:HIS13 3.2 30.1 1.0
HD2 A:HIS13 3.2 27.9 1.0
ND1 A:HIS13 4.1 24.1 1.0
CG A:HIS13 4.2 23.0 1.0
HA A:ARG14 4.6 29.2 1.0
HG2 A:ARG14 4.8 54.0 1.0
HD1 A:HIS13 4.9 28.9 1.0
HB A:THR17 5.0 30.8 1.0

Zinc binding site 2 out of 2 in 6t3d

Go back to Zinc Binding Sites List in 6t3d
Zinc binding site 2 out of 2 in the Crystal Structure of Ampc From E.Coli


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 within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Zn403

b:36.7
occ:0.45
O A:HOH691 2.0 42.8 0.5
O A:HOH510 2.0 33.2 0.5
O A:HOH749 2.1 39.1 0.5
O A:HOH562 2.1 34.6 0.5
NE2 A:HIS186 2.2 38.1 1.0
CE1 A:HIS186 3.2 42.8 1.0
CD2 A:HIS186 3.2 38.0 1.0
HE1 A:HIS186 3.3 51.3 1.0
HD2 A:HIS186 3.3 45.6 1.0
O A:HOH765 3.8 56.2 1.0
O A:HOH567 3.9 48.7 1.0
OE2 A:GLU195 4.0 59.6 1.0
ND1 A:HIS186 4.3 39.5 1.0
CG A:HIS186 4.3 33.4 1.0
OE1 A:GLU195 4.3 49.6 1.0
CD A:GLU195 4.6 60.9 1.0

Reference:

P.A.Lang, A.Parkova, T.M.Leissing, K.Calvopina, R.Cain, A.Krajnc, T.D.Panduwawala, J.Philippe, C.W.G.Fishwick, P.Trapencieris, M.G.P.Page, C.J.Schofield, J.Brem. Bicyclic Boronates As Potent Inhibitors of Ampc, the Class C Beta-Lactamase From Escherichia Coli Biomolecules 2020.
ISSN: ESSN 2218-273X
DOI: 10.3390/BIOM10060899
Page generated: Tue Oct 29 07:48:23 2024

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