Zinc in PDB 2fzc: The Structure of Wild-Type E. Coli Aspartate Transcarbamoylase in Complex with Novel T State Inhibitors at 2.10 Resolution

All present enzymatic activity of The Structure of Wild-Type E. Coli Aspartate Transcarbamoylase in Complex with Novel T State Inhibitors at 2.10 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 2.10 Resolution, PDB code: 2fzc 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)	27.35 / 2.10
Space group	P 3 2 1
Cell size a, b, c (Å), α, β, γ (°)	120.590, 120.590, 141.710, 90.00, 90.00, 120.00
R / Rfree (%)	19.6 / 25

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 2.10 Resolution (pdb code 2fzc). 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 2.10 Resolution, PDB code: 2fzc:
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 2.10 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 2.10 Resolution within 5.0Å range: probe atom residue distance (Å) B Occ B:Zn154 b:24.4 occ:1.00 SG B:CYS141 2.3 25.4 1.0 SG B:CYS114 2.3 26.6 1.0 SG B:CYS138 2.3 27.4 1.0 SG B:CYS109 2.4 27.8 1.0 CB B:CYS138 3.0 26.5 1.0 CB B:CYS114 3.1 22.8 1.0 CB B:CYS109 3.2 28.1 1.0 CB B:CYS141 3.4 21.6 1.0 N B:CYS141 3.8 20.9 1.0 CA B:CYS141 4.2 22.1 1.0 OG B:SER116 4.4 29.3 1.0 CA B:CYS114 4.5 23.8 1.0 CA B:CYS138 4.5 27.7 1.0 CB B:ASN111 4.6 25.3 1.0 CB B:TYR140 4.6 28.1 1.0 CA B:CYS109 4.7 26.2 1.0 ND2 B:ASN111 4.8 23.4 1.0 O B:HOH917 4.9 29.5 1.0 C B:TYR140 4.9 23.7 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 2.10 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 2.10 Resolution within 5.0Å range: probe atom residue distance (Å) B Occ D:Zn154 b:29.3 occ:1.00 SG D:CYS109 2.3 24.3 1.0 SG D:CYS138 2.3 24.6 1.0 SG D:CYS114 2.4 21.6 1.0 SG D:CYS141 2.4 26.4 1.0 CB D:CYS138 3.1 22.6 1.0 CB D:CYS109 3.2 24.7 1.0 CB D:CYS114 3.2 19.0 1.0 CB D:CYS141 3.3 25.1 1.0 N D:CYS141 3.6 21.0 1.0 CA D:CYS141 4.0 26.3 1.0 OG D:SER116 4.4 31.6 1.0 CA D:CYS114 4.5 23.8 1.0 CB D:ASN111 4.6 25.8 1.0 CA D:CYS138 4.6 26.8 1.0 CA D:CYS109 4.6 25.3 1.0 CB D:TYR140 4.7 22.8 1.0 C D:TYR140 4.8 24.1 1.0 O D:HOH1011 4.8 20.1 1.0 ND2 D:ASN111 4.9 27.7 1.0 C D:CYS141 4.9 24.9 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