Zinc in PDB 2fzg: The Structure of Wild-Type E. Coli Aspartate Transcarbamoylase in Complex with Novel T State Inhibitors at 2.25 Resolution

All present enzymatic activity of The Structure of Wild-Type E. Coli Aspartate Transcarbamoylase in Complex with Novel T State Inhibitors at 2.25 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 2.25 Resolution, PDB code: 2fzg 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)	28.23 / 2.25
Space group	P 3 2 1
Cell size a, b, c (Å), α, β, γ (°)	119.940, 119.940, 141.970, 90.00, 90.00, 120.00
R / Rfree (%)	20.1 / 23.7

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 2.25 Resolution (pdb code 2fzg). 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 2.25 Resolution, PDB code: 2fzg:
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 2.25 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 2.25 Resolution within 5.0Å range: probe atom residue distance (Å) B Occ B:Zn154 b:42.0 occ:1.00 SG B:CYS141 1.4 36.5 1.0 SG B:CYS114 2.2 26.9 1.0 CB B:CYS141 2.3 23.0 1.0 SG B:CYS109 2.4 29.6 1.0 SG B:CYS138 2.5 32.1 1.0 CB B:CYS114 2.8 21.0 1.0 CB B:CYS109 3.1 29.7 1.0 N B:CYS141 3.2 26.8 1.0 CA B:CYS141 3.3 28.8 1.0 CB B:CYS138 3.7 32.0 1.0 O B:HOH984 4.0 78.5 1.0 CA B:CYS114 4.1 24.0 1.0 OG B:SER116 4.2 19.4 1.0 C B:TYR140 4.5 27.1 1.0 CB B:TYR140 4.5 27.4 1.0 CA B:CYS109 4.6 30.6 1.0 O B:HOH911 4.6 34.5 1.0 ND2 B:ASN111 4.6 26.6 1.0 C B:CYS141 4.7 27.9 1.0 CB B:ASN111 4.7 26.6 1.0 CB B:SER116 4.8 25.7 1.0 C B:CYS114 4.9 23.7 1.0 CA B:TYR140 4.9 27.6 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 2.25 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 2.25 Resolution within 5.0Å range: probe atom residue distance (Å) B Occ D:Zn154 b:28.4 occ:1.00 SG D:CYS141 2.1 35.7 1.0 SG D:CYS109 2.2 37.6 1.0 SG D:CYS138 2.3 20.2 1.0 SG D:CYS114 2.4 22.2 1.0 CB D:CYS109 2.7 32.1 1.0 CB D:CYS141 2.8 23.7 1.0 CB D:CYS114 3.1 21.9 1.0 CB D:CYS138 3.2 25.1 1.0 N D:CYS141 3.4 23.0 1.0 CA D:CYS141 3.7 23.1 1.0 CA D:CYS109 4.1 34.3 1.0 CA D:CYS114 4.4 21.9 1.0 CB D:ASN111 4.5 23.7 1.0 OG D:SER116 4.5 26.5 1.0 C D:TYR140 4.6 23.3 1.0 CA D:CYS138 4.6 26.4 1.0 CB D:TYR140 4.6 23.6 1.0 O D:HOH907 4.7 25.9 1.0 ND2 D:ASN111 4.7 18.4 1.0 C D:CYS141 4.8 22.6 1.0 CA D:TYR140 4.9 24.6 1.0 N D:TYR140 4.9 25.6 1.0 C D:CYS109 5.0 35.9 1.0 CB D:SER116 5.0 31.5 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