Zinc in PDB 2fzk: The Structure of Wild-Type E. Coli Aspartate Transcarbamoylase in Complex with Novel T State Inhibitors at 2.50 Resolution

All present enzymatic activity of The Structure of Wild-Type E. Coli Aspartate Transcarbamoylase in Complex with Novel T State Inhibitors at 2.50 Resolution:
2.1.3.2;

The structure of The Structure of Wild-Type E. Coli Aspartate Transcarbamoylase in Complex with Novel T State Inhibitors at 2.50 Resolution, PDB code: 2fzk was solved by S.Heng, K.A.Stieglitz, J.Eldo, J.Xia, J.P.Cardia, E.R.Kantrowitz, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	28.45 / 2.50
Space group	P 3 2 1
Cell size a, b, c (Å), α, β, γ (°)	120.900, 120.900, 141.610, 90.00, 90.00, 120.00
R / Rfree (%)	21.1 / 23.9

The binding sites of Zinc atom in the The Structure of Wild-Type E. Coli Aspartate Transcarbamoylase in Complex with Novel T State Inhibitors at 2.50 Resolution (pdb code 2fzk). This binding sites where shown within 5.0 Angstroms radius around Zinc atom.
In total 2 binding sites of Zinc where determined in the The Structure of Wild-Type E. Coli Aspartate Transcarbamoylase in Complex with Novel T State Inhibitors at 2.50 Resolution, PDB code: 2fzk:
Jump to Zinc binding site number: 1; 2;

Zinc binding site 1 out of 2 in the The Structure of Wild-Type E. Coli Aspartate Transcarbamoylase in Complex with Novel T State Inhibitors at 2.50 Resolution


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 1 of The Structure of Wild-Type E. Coli Aspartate Transcarbamoylase in Complex with Novel T State Inhibitors at 2.50 Resolution within 5.0Å range: probe atom residue distance (Å) B Occ B:Zn154 b:50.4 occ:1.00 SG B:CYS109 2.2 46.1 1.0 SG B:CYS141 2.2 45.2 1.0 SG B:CYS114 2.3 35.2 1.0 SG B:CYS138 2.5 39.2 1.0 CB B:CYS138 2.9 37.8 1.0 CB B:CYS114 3.0 29.3 1.0 CB B:CYS141 3.2 42.4 1.0 CB B:CYS109 3.2 40.7 1.0 N B:CYS141 3.5 30.6 1.0 CA B:CYS141 4.0 36.5 1.0 ND2 B:ASN111 4.3 33.6 1.0 CA B:CYS114 4.3 31.6 1.0 CB B:ASN111 4.4 34.4 1.0 CA B:CYS138 4.4 41.6 1.0 OG B:SER116 4.6 30.7 1.0 CB B:TYR140 4.6 32.2 1.0 CA B:CYS109 4.7 41.4 1.0 C B:TYR140 4.7 29.5 1.0 CG B:ASN111 4.9 37.1 1.0 C B:CYS141 4.9 39.2 1.0 C B:CYS138 4.9 38.4 1.0 CA B:TYR140 5.0 31.6 1.0 N B:TYR140 5.0 33.5 1.0

Zinc binding site 2 out of 2 in the The Structure of Wild-Type E. Coli Aspartate Transcarbamoylase in Complex with Novel T State Inhibitors at 2.50 Resolution


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 2 of The Structure of Wild-Type E. Coli Aspartate Transcarbamoylase in Complex with Novel T State Inhibitors at 2.50 Resolution within 5.0Å range: probe atom residue distance (Å) B Occ D:Zn154 b:51.0 occ:1.00 SG D:CYS114 2.2 27.3 1.0 SG D:CYS109 2.3 48.8 1.0 SG D:CYS138 2.3 40.0 1.0 SG D:CYS141 2.5 45.1 1.0 CB D:CYS138 3.0 40.4 1.0 CB D:CYS109 3.3 40.0 1.0 CB D:CYS114 3.3 29.7 1.0 CB D:CYS141 3.3 34.3 1.0 N D:CYS141 3.5 33.2 1.0 CA D:CYS141 4.0 35.9 1.0 CB D:ASN111 4.3 19.9 1.0 OG D:SER116 4.3 39.8 1.0 CB D:TYR140 4.4 33.4 1.0 CA D:CYS114 4.4 30.6 1.0 CA D:CYS138 4.5 40.9 1.0 C D:TYR140 4.6 34.3 1.0 CA D:CYS109 4.7 39.4 1.0 O D:HOH906 4.8 24.9 1.0 ND2 D:ASN111 4.8 15.0 1.0 C D:CYS141 4.8 34.5 1.0 CE1 D:PHE145 4.9 43.6 1.0 CA D:TYR140 4.9 34.5 1.0 N D:GLU142 4.9 32.4 1.0 N D:TYR140 4.9 37.5 1.0 CB D:SER116 5.0 38.6 1.0

S.Heng, K.A.Stieglitz, J.Eldo, J.Xia, J.P.Cardia, E.R.Kantrowitz. T-State Inhibitors of E. Coli Aspartate Transcarbamoylase That Prevent the Allosteric Transition. Biochemistry V. 45 10062 2006.
ISSN: ISSN 0006-2960
PubMed: 16906764
DOI: 10.1021/BI0601095